ACAC_YEAST
ID ACAC_YEAST Reviewed; 2233 AA.
AC Q00955; D6W1J1;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=Acetyl-CoA carboxylase;
DE Short=ACC;
DE EC=6.4.1.2 {ECO:0000269|PubMed:12663926, ECO:0000269|PubMed:15079078};
DE AltName: Full=Fatty acid synthetase 3;
DE AltName: Full=mRNA transport-defective protein 7;
DE Includes:
DE RecName: Full=Biotin carboxylase;
DE EC=6.3.4.14;
GN Name=ACC1; Synonyms=ABP2, FAS3, MTR7; OrderedLocusNames=YNR016C;
GN ORFNames=N3175;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2015-2022.
RX PubMed=1350093; DOI=10.1073/pnas.89.10.4534;
RA Al-Feel W., Chirala S.S., Wakil S.J.;
RT "Cloning of the yeast FAS3 gene and primary structure of yeast acetyl-CoA
RT carboxylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4534-4538(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=6108218; DOI=10.1111/j.1432-1033.1980.tb06077.x;
RA Mishina M., Roggenkamp R., Schweizer E.;
RT "Yeast mutants defective in acetyl-coenzyme A carboxylase and biotin:
RT apocarboxylase ligase.";
RL Eur. J. Biochem. 111:79-87(1980).
RN [5]
RP FUNCTION.
RX PubMed=6103540; DOI=10.1073/pnas.77.4.1814;
RA Roggenkamp R., Numa S., Schweizer E.;
RT "Fatty acid-requiring mutant of Saccharomyces cerevisiae defective in
RT acetyl-CoA carboxylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:1814-1817(1980).
RN [6]
RP INDUCTION.
RX PubMed=1359536; DOI=10.1073/pnas.89.21.10232;
RA Chirala S.S.;
RT "Coordinated regulation and inositol-mediated and fatty acid-mediated
RT repression of fatty acid synthase genes in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10232-10236(1992).
RN [7]
RP INDUCTION.
RX PubMed=8098706; DOI=10.1016/s0021-9258(18)82077-4;
RA Hasslacher M., Ivessa A.S., Paltauf F., Kohlwein S.D.;
RT "Acetyl-CoA carboxylase from yeast is an essential enzyme and is regulated
RT by factors that control phospholipid metabolism.";
RL J. Biol. Chem. 268:10946-10952(1993).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=7916271; DOI=10.1007/bf00309532;
RA Vahlensieck H.F., Pridzun L., Reichenbach H., Hinnen A.;
RT "Identification of the yeast ACC1 gene product (acetyl-CoA carboxylase) as
RT the target of the polyketide fungicide soraphen A.";
RL Curr. Genet. 25:95-100(1994).
RN [9]
RP INDUCTION.
RX PubMed=8127678; DOI=10.1093/nar/22.3.412;
RA Chirala S.S., Zhong Q., Huang W., al-Feel W.;
RT "Analysis of FAS3/ACC regulatory region of Saccharomyces cerevisiae:
RT identification of a functional UASINO and sequences responsible for fatty
RT acid mediated repression.";
RL Nucleic Acids Res. 22:412-418(1994).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8943372; DOI=10.1128/mcb.16.12.7161;
RA Schneiter R., Hitomi M., Ivessa A.S., Fasch E.V., Kohlwein S.D.,
RA Tartakoff A.M.;
RT "A yeast acetyl coenzyme A carboxylase mutant links very-long-chain fatty
RT acid synthesis to the structure and function of the nuclear membrane-pore
RT complex.";
RL Mol. Cell. Biol. 16:7161-7172(1996).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=9438137;
RA Ivessa A.S., Schneiter R., Kohlwein S.D.;
RT "Yeast acetyl-CoA carboxylase is associated with the cytoplasmic surface of
RT the endoplasmic reticulum.";
RL Eur. J. Cell Biol. 74:399-406(1997).
RN [12]
RP FUNCTION.
RX PubMed=10757783; DOI=10.1128/mcb.20.9.2984-2995.2000;
RA Schneiter R., Guerra C.E., Lampl M., Tatzer V., Zellnig G., Klein H.L.,
RA Kohlwein S.D.;
RT "A novel cold-sensitive allele of the rate-limiting enzyme of fatty acid
RT synthesis, acetyl coenzyme A carboxylase, affects the morphology of the
RT yeast vacuole through acylation of Vac8p.";
RL Mol. Cell. Biol. 20:2984-2995(2000).
RN [13]
RP FUNCTION.
RX PubMed=12730220; DOI=10.1074/jbc.m301607200;
RA Gao H., Sumanaweera N., Bailer S.M., Stochaj U.;
RT "Nuclear accumulation of the small GTPase Gsp1p depends on nucleoporins
RT Nup133p, Rat2p/Nup120p, Nup85p, Nic96p, and the acetyl-CoA carboxylase
RT Acc1p.";
RL J. Biol. Chem. 278:25331-25340(2003).
RN [14]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2; SER-1148 AND SER-1157, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1157, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1148 AND SER-1157, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-790; SER-1148; SER-1157 AND
RP SER-1162, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1429-2233 IN COMPLEX WITH COA,
RP CATALYTIC ACTIVITY AS ACETYL-COA CARBOXYLASE, MUTAGENESIS OF LEU-1705;
RP ARG-1731; TYR-1738; ARG-1954; GLU-1994; GLU-2026 AND ARG-2036, AND
RP HOMODIMERIZATION.
RX PubMed=12663926; DOI=10.1126/science.1081366;
RA Zhang H., Yang Z., Shen Y., Tong L.;
RT "Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A
RT carboxylase.";
RL Science 299:2064-2067(2003).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 13-566 IN COMPLEX WITH SORAPHEN,
RP AND SUBUNIT.
RX PubMed=15610732; DOI=10.1016/j.molcel.2004.11.034;
RA Shen Y., Volrath S.L., Weatherly S.C., Elich T.D., Tong L.;
RT "A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A
RT carboxylase by soraphen A, a macrocyclic polyketide natural product.";
RL Mol. Cell 16:881-891(2004).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1482-2218 IN COMPLEXES WITH THE
RP INHIBITORS HALOXYFOP OR DICLOFOP, SUBUNIT, AND CATALYTIC ACTIVITY AS
RP ACETYL-COA CARBOXYLASE.
RX PubMed=15079078; DOI=10.1073/pnas.0400891101;
RA Zhang H., Tweel B., Tong L.;
RT "Molecular basis for the inhibition of the carboxyltransferase domain of
RT acetyl-coenzyme-A carboxylase by haloxyfop and diclofop.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5910-5915(2004).
CC -!- FUNCTION: Carries out three functions: biotin carboxyl carrier protein,
CC biotin carboxylase and carboxyltransferase. Involved in the synthesis
CC of very-long-chain fatty acid synthesis which is required to maintain a
CC functional nuclear envelope. Required for acylation and vacuolar
CC membrane association of VAC8 which is necessary to maintain a normal
CC morphology of the vacuole. {ECO:0000269|PubMed:10757783,
CC ECO:0000269|PubMed:12730220, ECO:0000269|PubMed:6103540,
CC ECO:0000269|PubMed:6108218, ECO:0000269|PubMed:8943372}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-
CC CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;
CC Evidence={ECO:0000269|PubMed:12663926, ECO:0000269|PubMed:15079078};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC ChEBI:CHEBI:456216; EC=6.3.4.14;
CC Evidence={ECO:0000250|UniProtKB:Q5SWU9};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000250|UniProtKB:O00763};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: By phosphorylation. The catalytic activity is
CC inhibited by soraphen A, a polyketide isolated from the myxobacterium
CC Sorangium cellulosum and a potent inhibitor of fungal growth.
CC {ECO:0000269|PubMed:7916271}.
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12663926,
CC ECO:0000269|PubMed:15079078, ECO:0000269|PubMed:15610732}.
CC -!- INTERACTION:
CC Q00955; Q00955: ACC1; NbExp=4; IntAct=EBI-4814, EBI-4814;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum membrane;
CC Peripheral membrane protein; Cytoplasmic side.
CC -!- INDUCTION: Repressed in presence of fatty acids. Repressed 3-fold by
CC lipid precursors, inositol and choline, and also controlled by
CC regulatory factors INO2, INO4 and OPI1. {ECO:0000269|PubMed:1359536,
CC ECO:0000269|PubMed:8098706, ECO:0000269|PubMed:8127678}.
CC -!- MISCELLANEOUS: Present with 20200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; M92156; AAA20073.1; -; Genomic_DNA.
DR EMBL; Z71631; CAA96294.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10557.1; -; Genomic_DNA.
DR PIR; S63347; S63347.
DR RefSeq; NP_014413.1; NM_001183193.1.
DR PDB; 1OD2; X-ray; 2.70 A; A/B=1429-2233.
DR PDB; 1OD4; X-ray; 2.70 A; A/B/C=1429-2233.
DR PDB; 1UYR; X-ray; 2.50 A; A/B=1482-2218.
DR PDB; 1UYS; X-ray; 2.80 A; A/B/C=1482-2218.
DR PDB; 1UYT; X-ray; 2.50 A; A/B/C=1482-2218.
DR PDB; 1UYV; X-ray; 2.60 A; A/B/C=1482-2218.
DR PDB; 1W2X; X-ray; 2.80 A; A/B/C=1476-2233.
DR PDB; 1W93; X-ray; 2.50 A; A=14-566.
DR PDB; 1W96; X-ray; 1.80 A; A/B/C=13-566.
DR PDB; 3H0J; X-ray; 2.80 A; A/B/C=1476-2233.
DR PDB; 3H0Q; X-ray; 2.50 A; A/B/C=1476-2233.
DR PDB; 3H0S; X-ray; 2.43 A; A/B/C=1476-2233.
DR PDB; 3K8X; X-ray; 2.30 A; A/B/C=1476-2233.
DR PDB; 3PGQ; X-ray; 2.80 A; A/B/C=1476-2233.
DR PDB; 3TV5; X-ray; 2.80 A; A/B/C=1476-2233.
DR PDB; 3TVU; X-ray; 2.40 A; A/B/C=1476-2233.
DR PDB; 3TVW; X-ray; 2.80 A; A/B/C=1476-2233.
DR PDB; 3TZ3; X-ray; 2.70 A; A/B/C=1476-2233.
DR PDB; 4WYO; X-ray; 2.89 A; B/C=1476-2233.
DR PDB; 4WZ8; X-ray; 2.23 A; B/C=1476-2233.
DR PDB; 5CS0; X-ray; 2.50 A; A/B=797-1033.
DR PDB; 5CS4; X-ray; 3.19 A; A/B=1036-1503.
DR PDB; 5CSA; X-ray; 3.00 A; A/B=569-1494.
DR PDB; 5CSK; X-ray; 3.10 A; A/B=22-2233.
DR PDB; 5CSL; X-ray; 3.20 A; A/B=22-2233.
DR PDB; 5CTB; X-ray; 2.40 A; A/B/C=1476-2233.
DR PDB; 5CTC; X-ray; 2.70 A; A/B/C=1476-2233.
DR PDB; 5CTE; X-ray; 2.34 A; B/C=1476-2233.
DR PDB; 5I6E; X-ray; 3.00 A; A=768-1494.
DR PDB; 5TRC; X-ray; 2.90 A; A/B=1036-1503.
DR PDBsum; 1OD2; -.
DR PDBsum; 1OD4; -.
DR PDBsum; 1UYR; -.
DR PDBsum; 1UYS; -.
DR PDBsum; 1UYT; -.
DR PDBsum; 1UYV; -.
DR PDBsum; 1W2X; -.
DR PDBsum; 1W93; -.
DR PDBsum; 1W96; -.
DR PDBsum; 3H0J; -.
DR PDBsum; 3H0Q; -.
DR PDBsum; 3H0S; -.
DR PDBsum; 3K8X; -.
DR PDBsum; 3PGQ; -.
DR PDBsum; 3TV5; -.
DR PDBsum; 3TVU; -.
DR PDBsum; 3TVW; -.
DR PDBsum; 3TZ3; -.
DR PDBsum; 4WYO; -.
DR PDBsum; 4WZ8; -.
DR PDBsum; 5CS0; -.
DR PDBsum; 5CS4; -.
DR PDBsum; 5CSA; -.
DR PDBsum; 5CSK; -.
DR PDBsum; 5CSL; -.
DR PDBsum; 5CTB; -.
DR PDBsum; 5CTC; -.
DR PDBsum; 5CTE; -.
DR PDBsum; 5I6E; -.
DR PDBsum; 5TRC; -.
DR AlphaFoldDB; Q00955; -.
DR SMR; Q00955; -.
DR BioGRID; 35841; 308.
DR DIP; DIP-975N; -.
DR IntAct; Q00955; 42.
DR MINT; Q00955; -.
DR STRING; 4932.YNR016C; -.
DR CarbonylDB; Q00955; -.
DR iPTMnet; Q00955; -.
DR MaxQB; Q00955; -.
DR PaxDb; Q00955; -.
DR PRIDE; Q00955; -.
DR EnsemblFungi; YNR016C_mRNA; YNR016C; YNR016C.
DR GeneID; 855750; -.
DR KEGG; sce:YNR016C; -.
DR SGD; S000005299; ACC1.
DR VEuPathDB; FungiDB:YNR016C; -.
DR eggNOG; KOG0368; Eukaryota.
DR GeneTree; ENSGT00940000175750; -.
DR HOGENOM; CLU_000395_5_2_1; -.
DR InParanoid; Q00955; -.
DR OMA; LIQCAMP; -.
DR BioCyc; YEAST:MON3O-7; -.
DR BRENDA; 6.3.4.14; 984.
DR BRENDA; 6.4.1.2; 984.
DR Reactome; R-SCE-163765; ChREBP activates metabolic gene expression.
DR Reactome; R-SCE-196780; Biotin transport and metabolism.
DR Reactome; R-SCE-200425; Carnitine metabolism.
DR Reactome; R-SCE-75105; Fatty acyl-CoA biosynthesis.
DR UniPathway; UPA00655; UER00711.
DR EvolutionaryTrace; Q00955; -.
DR PRO; PR:Q00955; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; Q00955; protein.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IMP:CAFA.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:1905502; F:acetyl-CoA binding; IMP:CAFA.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IMP:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004075; F:biotin carboxylase activity; IMP:SGD.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IMP:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IMP:CAFA.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IMP:CAFA.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IMP:SGD.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR DisProt; DP00557; -.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR013537; AcCoA_COase_cen.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF08326; ACC_central; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52096; SSF52096; 2.
DR SUPFAM; SSF52440; SSF52440; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Biotin; Cytoplasm;
KW Direct protein sequencing; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW Manganese; Membrane; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..2233
FT /note="Acetyl-CoA carboxylase"
FT /id="PRO_0000146770"
FT DOMAIN 58..567
FT /note="Biotin carboxylation"
FT DOMAIN 216..408
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 694..768
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 1486..1822
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 1826..2141
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 1486..2141
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT ACT_SITE 383
FT /evidence="ECO:0000250"
FT BINDING 256..261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 365
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 381
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1627..1629
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 1731
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 1998
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT BINDING 2034
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 2036
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 735
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT MOD_RES 790
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 1705
FT /note="L->I: Raises KM for malonyl-CoA by a factor of 20."
FT /evidence="ECO:0000269|PubMed:12663926"
FT MUTAGEN 1731
FT /note="R->S: Raises KM for malonyl-CoA by a factor of 15."
FT /evidence="ECO:0000269|PubMed:12663926"
FT MUTAGEN 1738
FT /note="Y->F: Does not affect catalytic activity."
FT /evidence="ECO:0000269|PubMed:12663926"
FT MUTAGEN 1954
FT /note="R->S: Raises KM for malonyl-CoA by a factor of 70."
FT /evidence="ECO:0000269|PubMed:12663926"
FT MUTAGEN 1994
FT /note="E->Q: Does not affect catalytic activity."
FT /evidence="ECO:0000269|PubMed:12663926"
FT MUTAGEN 2026
FT /note="E->Q: Does not affect catalytic activity."
FT /evidence="ECO:0000269|PubMed:12663926"
FT MUTAGEN 2036
FT /note="R->E: Affects only slightly binding of Co-A."
FT /evidence="ECO:0000269|PubMed:12663926"
FT CONFLICT 1523
FT /note="W -> G (in Ref. 1; AAA20073)"
FT /evidence="ECO:0000305"
FT CONFLICT 1755
FT /note="I -> IWYRCL (in Ref. 1; AAA20073)"
FT /evidence="ECO:0000305"
FT CONFLICT 1761..1766
FT /note="AINKML -> ESTNA (in Ref. 1; AAA20073)"
FT /evidence="ECO:0000305"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:1W96"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:1W96"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 68..86
FT /evidence="ECO:0007829|PDB:1W96"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:1W96"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1W96"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 131..140
FT /evidence="ECO:0007829|PDB:1W96"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:1W96"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:1W96"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 186..195
FT /evidence="ECO:0007829|PDB:1W96"
FT TURN 204..207
FT /evidence="ECO:0007829|PDB:1W96"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:1W96"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:1W96"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:1W96"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:1W96"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:1W96"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:1W96"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:1W93"
FT STRAND 311..323
FT /evidence="ECO:0007829|PDB:1W96"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 339..356
FT /evidence="ECO:0007829|PDB:1W96"
FT STRAND 360..368
FT /evidence="ECO:0007829|PDB:1W96"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:1W96"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 388..395
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 399..407
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 416..421
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 439..444
FT /evidence="ECO:0007829|PDB:1W96"
FT STRAND 452..462
FT /evidence="ECO:0007829|PDB:1W96"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:1W93"
FT STRAND 472..478
FT /evidence="ECO:0007829|PDB:1W96"
FT STRAND 484..492
FT /evidence="ECO:0007829|PDB:1W96"
FT STRAND 503..515
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 516..530
FT /evidence="ECO:0007829|PDB:1W96"
FT STRAND 531..536
FT /evidence="ECO:0007829|PDB:5CSK"
FT HELIX 541..547
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 550..553
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 561..565
FT /evidence="ECO:0007829|PDB:1W96"
FT HELIX 577..605
FT /evidence="ECO:0007829|PDB:5CSA"
FT HELIX 612..615
FT /evidence="ECO:0007829|PDB:5CSA"
FT STRAND 618..624
FT /evidence="ECO:0007829|PDB:5CSA"
FT STRAND 626..636
FT /evidence="ECO:0007829|PDB:5CSA"
FT STRAND 638..648
FT /evidence="ECO:0007829|PDB:5CSA"
FT STRAND 650..657
FT /evidence="ECO:0007829|PDB:5CSA"
FT STRAND 659..661
FT /evidence="ECO:0007829|PDB:5CSA"
FT STRAND 663..669
FT /evidence="ECO:0007829|PDB:5CSA"
FT STRAND 671..675
FT /evidence="ECO:0007829|PDB:5CSA"
FT STRAND 682..687
FT /evidence="ECO:0007829|PDB:5CSA"
FT STRAND 690..695
FT /evidence="ECO:0007829|PDB:5CSA"
FT STRAND 702..704
FT /evidence="ECO:0007829|PDB:5CSA"
FT STRAND 709..716
FT /evidence="ECO:0007829|PDB:5CSA"
FT STRAND 727..733
FT /evidence="ECO:0007829|PDB:5CSA"
FT STRAND 736..741
FT /evidence="ECO:0007829|PDB:5CSA"
FT STRAND 746..750
FT /evidence="ECO:0007829|PDB:5CSA"
FT STRAND 763..767
FT /evidence="ECO:0007829|PDB:5CSA"
FT HELIX 772..774
FT /evidence="ECO:0007829|PDB:5CSA"
FT STRAND 793..795
FT /evidence="ECO:0007829|PDB:5I6E"
FT HELIX 798..813
FT /evidence="ECO:0007829|PDB:5CS0"
FT HELIX 818..833
FT /evidence="ECO:0007829|PDB:5CS0"
FT HELIX 838..850
FT /evidence="ECO:0007829|PDB:5CS0"
FT HELIX 851..853
FT /evidence="ECO:0007829|PDB:5CS0"
FT HELIX 856..871
FT /evidence="ECO:0007829|PDB:5CS0"
FT HELIX 878..889
FT /evidence="ECO:0007829|PDB:5CS0"
FT TURN 892..894
FT /evidence="ECO:0007829|PDB:5CS0"
FT STRAND 896..898
FT /evidence="ECO:0007829|PDB:5CS0"
FT HELIX 900..913
FT /evidence="ECO:0007829|PDB:5CS0"
FT TURN 914..916
FT /evidence="ECO:0007829|PDB:5CS0"
FT HELIX 918..937
FT /evidence="ECO:0007829|PDB:5CS0"
FT HELIX 938..940
FT /evidence="ECO:0007829|PDB:5CSA"
FT STRAND 942..944
FT /evidence="ECO:0007829|PDB:5CSL"
FT HELIX 947..957
FT /evidence="ECO:0007829|PDB:5CSA"
FT HELIX 962..972
FT /evidence="ECO:0007829|PDB:5CS0"
FT HELIX 975..995
FT /evidence="ECO:0007829|PDB:5CS0"
FT HELIX 997..1002
FT /evidence="ECO:0007829|PDB:5CS0"
FT HELIX 1004..1011
FT /evidence="ECO:0007829|PDB:5CS0"
FT HELIX 1016..1018
FT /evidence="ECO:0007829|PDB:5CS0"
FT HELIX 1019..1030
FT /evidence="ECO:0007829|PDB:5CS0"
FT HELIX 1037..1052
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1054..1056
FT /evidence="ECO:0007829|PDB:5CSA"
FT STRAND 1057..1059
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1062..1066
FT /evidence="ECO:0007829|PDB:5CSA"
FT HELIX 1069..1076
FT /evidence="ECO:0007829|PDB:5TRC"
FT HELIX 1083..1086
FT /evidence="ECO:0007829|PDB:5TRC"
FT HELIX 1087..1090
FT /evidence="ECO:0007829|PDB:5TRC"
FT TURN 1095..1097
FT /evidence="ECO:0007829|PDB:5TRC"
FT HELIX 1098..1109
FT /evidence="ECO:0007829|PDB:5TRC"
FT TURN 1110..1112
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1113..1122
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1124..1134
FT /evidence="ECO:0007829|PDB:5TRC"
FT HELIX 1138..1140
FT /evidence="ECO:0007829|PDB:5I6E"
FT STRAND 1155..1157
FT /evidence="ECO:0007829|PDB:5CSL"
FT HELIX 1158..1160
FT /evidence="ECO:0007829|PDB:5CSL"
FT STRAND 1167..1170
FT /evidence="ECO:0007829|PDB:5I6E"
FT STRAND 1173..1178
FT /evidence="ECO:0007829|PDB:5TRC"
FT HELIX 1183..1185
FT /evidence="ECO:0007829|PDB:5TRC"
FT HELIX 1186..1194
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1220..1225
FT /evidence="ECO:0007829|PDB:5TRC"
FT HELIX 1235..1255
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1258..1265
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1268..1270
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1274..1279
FT /evidence="ECO:0007829|PDB:5TRC"
FT TURN 1280..1283
FT /evidence="ECO:0007829|PDB:5TRC"
FT HELIX 1287..1289
FT /evidence="ECO:0007829|PDB:5TRC"
FT HELIX 1294..1300
FT /evidence="ECO:0007829|PDB:5TRC"
FT HELIX 1303..1305
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1308..1313
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1320..1327
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1334..1342
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1349..1351
FT /evidence="ECO:0007829|PDB:5TRC"
FT HELIX 1353..1372
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1378..1380
FT /evidence="ECO:0007829|PDB:5I6E"
FT STRAND 1382..1389
FT /evidence="ECO:0007829|PDB:5TRC"
FT HELIX 1397..1403
FT /evidence="ECO:0007829|PDB:5TRC"
FT TURN 1404..1408
FT /evidence="ECO:0007829|PDB:5TRC"
FT HELIX 1409..1411
FT /evidence="ECO:0007829|PDB:5TRC"
FT HELIX 1412..1418
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1420..1430
FT /evidence="ECO:0007829|PDB:5TRC"
FT TURN 1432..1434
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1437..1445
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1447..1450
FT /evidence="ECO:0007829|PDB:5I6E"
FT STRAND 1453..1461
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1463..1465
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1467..1474
FT /evidence="ECO:0007829|PDB:5TRC"
FT TURN 1477..1480
FT /evidence="ECO:0007829|PDB:5TRC"
FT STRAND 1482..1484
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 1490..1493
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 1495..1502
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 1508..1510
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 1511..1526
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 1534..1536
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1537..1544
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1546..1548
FT /evidence="ECO:0007829|PDB:1OD2"
FT STRAND 1550..1553
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1561..1571
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1580..1587
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 1592..1594
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 1598..1614
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1618..1622
FT /evidence="ECO:0007829|PDB:4WZ8"
FT TURN 1633..1638
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1640..1645
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 1649..1651
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1653..1658
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 1660..1668
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 1672..1674
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1675..1682
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1685..1693
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1696..1698
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 1702..1719
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1724..1728
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 1735..1742
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1745..1749
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1754..1757
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 1759..1766
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 1775..1778
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 1780..1783
FT /evidence="ECO:0007829|PDB:4WZ8"
FT TURN 1784..1787
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1788..1795
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 1796..1807
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1812..1816
FT /evidence="ECO:0007829|PDB:5CSK"
FT STRAND 1827..1829
FT /evidence="ECO:0007829|PDB:5CTE"
FT STRAND 1837..1839
FT /evidence="ECO:0007829|PDB:3K8X"
FT HELIX 1843..1848
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1850..1852
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1855..1857
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1867..1870
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1877..1884
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1887..1894
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1899..1903
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1909..1911
FT /evidence="ECO:0007829|PDB:1OD4"
FT STRAND 1915..1919
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 1926..1940
FT /evidence="ECO:0007829|PDB:4WZ8"
FT TURN 1941..1943
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1947..1950
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1953..1956
FT /evidence="ECO:0007829|PDB:5CTE"
FT HELIX 1960..1964
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 1967..1979
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1985..1989
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 1994..1996
FT /evidence="ECO:0007829|PDB:3K8X"
FT HELIX 1997..2000
FT /evidence="ECO:0007829|PDB:4WZ8"
FT TURN 2001..2003
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 2005..2008
FT /evidence="ECO:0007829|PDB:4WZ8"
FT TURN 2009..2011
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 2012..2017
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 2021..2025
FT /evidence="ECO:0007829|PDB:3K8X"
FT HELIX 2027..2034
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 2039..2047
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 2049..2058
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 2059..2063
FT /evidence="ECO:0007829|PDB:5CTB"
FT HELIX 2065..2072
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 2078..2095
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 2100..2106
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 2108..2113
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 2115..2117
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 2118..2139
FT /evidence="ECO:0007829|PDB:4WZ8"
FT STRAND 2142..2144
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 2148..2157
FT /evidence="ECO:0007829|PDB:4WZ8"
FT HELIX 2168..2186
FT /evidence="ECO:0007829|PDB:4WZ8"
FT TURN 2189..2191
FT /evidence="ECO:0007829|PDB:3TVU"
FT TURN 2196..2199
FT /evidence="ECO:0007829|PDB:1UYV"
FT TURN 2203..2205
FT /evidence="ECO:0007829|PDB:1UYR"
FT HELIX 2206..2215
FT /evidence="ECO:0007829|PDB:5CTE"
FT HELIX 2223..2233
FT /evidence="ECO:0007829|PDB:5CTE"
SQ SEQUENCE 2233 AA; 250353 MW; 0A335AAD9B1F8308 CRC64;
MSEESLFESS PQKMEYEITN YSERHTELPG HFIGLNTVDK LEESPLRDFV KSHGGHTVIS
KILIANNGIA AVKEIRSVRK WAYETFGDDR TVQFVAMATP EDLEANAEYI RMADQYIEVP
GGTNNNNYAN VDLIVDIAER ADVDAVWAGW GHASENPLLP EKLSQSKRKV IFIGPPGNAM
RSLGDKISST IVAQSAKVPC IPWSGTGVDT VHVDEKTGLV SVDDDIYQKG CCTSPEDGLQ
KAKRIGFPVM IKASEGGGGK GIRQVEREED FIALYHQAAN EIPGSPIFIM KLAGRARHLE
VQLLADQYGT NISLFGRDCS VQRRHQKIIE EAPVTIAKAE TFHEMEKAAV RLGKLVGYVS
AGTVEYLYSH DDGKFYFLEL NPRLQVEHPT TEMVSGVNLP AAQLQIAMGI PMHRISDIRT
LYGMNPHSAS EIDFEFKTQD ATKKQRRPIP KGHCTACRIT SEDPNDGFKP SGGTLHELNF
RSSSNVWGYF SVGNNGNIHS FSDSQFGHIF AFGENRQASR KHMVVALKEL SIRGDFRTTV
EYLIKLLETE DFEDNTITTG WLDDLITHKM TAEKPDPTLA VICGAATKAF LASEEARHKY
IESLQKGQVL SKDLLQTMFP VDFIHEGKRY KFTVAKSGND RYTLFINGSK CDIILRQLSD
GGLLIAIGGK SHTIYWKEEV AATRLSVDSM TTLLEVENDP TQLRTPSPGK LVKFLVENGE
HIIKGQPYAE IEVMKMQMPL VSQENGIVQL LKQPGSTIVA GDIMAIMTLD DPSKVKHALP
FEGMLPDFGS PVIEGTKPAY KFKSLVSTLE NILKGYDNQV IMNASLQQLI EVLRNPKLPY
SEWKLHISAL HSRLPAKLDE QMEELVARSL RRGAVFPARQ LSKLIDMAVK NPEYNPDKLL
GAVVEPLADI AHKYSNGLEA HEHSIFVHFL EEYYEVEKLF NGPNVREENI ILKLRDENPK
DLDKVALTVL SHSKVSAKNN LILAILKHYQ PLCKLSSKVS AIFSTPLQHI VELESKATAK
VALQAREILI QGALPSVKER TEQIEHILKS SVVKVAYGSS NPKRSEPDLN ILKDLIDSNY
VVFDVLLQFL THQDPVVTAA AAQVYIRRAY RAYTIGDIRV HEGVTVPIVE WKFQLPSAAF
STFPTVKSKM GMNRAVSVSD LSYVANSQSS PLREGILMAV DHLDDVDEIL SQSLEVIPRH
QSSSNGPAPD RSGSSASLSN VANVCVASTE GFESEEEILV RLREILDLNK QELINASIRR
ITFMFGFKDG SYPKYYTFNG PNYNENETIR HIEPALAFQL ELGRLSNFNI KPIFTDNRNI
HVYEAVSKTS PLDKRFFTRG IIRTGHIRDD ISIQEYLTSE ANRLMSDILD NLEVTDTSNS
DLNHIFINFI AVFDISPEDV EAAFGGFLER FGKRLLRLRV SSAEIRIIIK DPQTGAPVPL
RALINNVSGY VIKTEMYTEV KNAKGEWVFK SLGKPGSMHL RPIATPYPVK EWLQPKRYKA
HLMGTTYVYD FPELFRQASS SQWKNFSADV KLTDDFFISN ELIEDENGEL TEVEREPGAN
AIGMVAFKIT VKTPEYPRGR QFVVVANDIT FKIGSFGPQE DEFFNKVTEY ARKRGIPRIY
LAANSGARIG MAEEIVPLFQ VAWNDAANPD KGFQYLYLTS EGMETLKKFD KENSVLTERT
VINGEERFVI KTIIGSEDGL GVECLRGSGL IAGATSRAYH DIFTITLVTC RSVGIGAYLV
RLGQRAIQVE GQPIILTGAP AINKMLGREV YTSNLQLGGT QIMYNNGVSH LTAVDDLAGV
EKIVEWMSYV PAKRNMPVPI LETKDTWDRP VDFTPTNDET YDVRWMIEGR ETESGFEYGL
FDKGSFFETL SGWAKGVVVG RARLGGIPLG VIGVETRTVE NLIPADPANP NSAETLIQEP
GQVWHPNSAF KTAQAINDFN NGEQLPMMIL ANWRGFSGGQ RDMFNEVLKY GSFIVDALVD
YKQPIIIYIP PTGELRGGSW VVVDPTINAD QMEMYADVNA RAGVLEPQGM VGIKFRREKL
LDTMNRLDDK YRELRSQLSN KSLAPEVHQQ ISKQLADRER ELLPIYGQIS LQFADLHDRS
SRMVAKGVIS KELEWTEARR FFFWRLRRRL NEEYLIKRLS HQVGEASRLE KIARIRSWYP
ASVDHEDDRQ VATWIEENYK TLDDKLKGLK LESFAQDLAK KIRSDHDNAI DGLSEVIKML
STDDKEKLLK TLK
