ACCC_ECOLI
ID ACCC_ECOLI Reviewed; 449 AA.
AC P24182; Q2M8V9;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Biotin carboxylase;
DE EC=6.3.4.14 {ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731};
DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000305};
GN Name=accC; Synonyms=fabG; OrderedLocusNames=b3256, JW3224;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=K12;
RX PubMed=1682920; DOI=10.1073/pnas.88.21.9730;
RA Kondo H., Shiratsuchi K., Yoshimoto T., Masuda T., Kitazono A., Tsuru D.,
RA Anai M., Sekiguchi M., Tanabe T.;
RT "Acetyl-CoA carboxylase from Escherichia coli: gene organization and
RT nucleotide sequence of the biotin carboxylase subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9730-9733(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1370469; DOI=10.1016/s0021-9258(18)48362-7;
RA Li S.-J., Cronan J.E. Jr.;
RT "The gene encoding the biotin carboxylase subunit of Escherichia coli
RT acetyl-CoA carboxylase.";
RL J. Biol. Chem. 267:855-863(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Best E.A., Knauf V.C.;
RT "Cloning and characterization of the E. coli fabEG operon encoding subunits
RT of acetyl-CoA carboxylase.";
RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-160.
RX PubMed=2575489; DOI=10.1089/dna.1989.8.779;
RA Alix J.-H.;
RT "A rapid procedure for cloning genes from lambda libraries by
RT complementation of E. coli defective mutants: application to the fabE
RT region of the E. coli chromosome.";
RL DNA 8:779-789(1989).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=7915138; DOI=10.1021/bi00200a004;
RA Waldrop G.L., Rayment I., Holden H.M.;
RT "Three-dimensional structure of the biotin carboxylase subunit of acetyl-
RT CoA carboxylase.";
RL Biochemistry 33:10249-10256(1994).
RN [9] {ECO:0007744|PDB:1DV1, ECO:0007744|PDB:1DV2}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ATP.
RX PubMed=10821865; DOI=10.1074/jbc.275.21.16183;
RA Thoden J.B., Blanchard C.Z., Holden H.M., Waldrop G.L.;
RT "Movement of the biotin carboxylase B-domain as a result of ATP binding.";
RL J. Biol. Chem. 275:16183-16190(2000).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF ARG-19; GLU-23;
RP PHE-363 AND ARG-366.
RX PubMed=16793549; DOI=10.1016/j.molcel.2006.04.026;
RA Shen Y., Chou C.-Y., Chang G.-G., Tong L.;
RT "Is dimerization required for the catalytic activity of bacterial biotin
RT carboxylase?";
RL Mol. Cell 22:807-818(2006).
RN [11] {ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-444 WILD TYPE AND MUTANT A-296
RP IN COMPLEX WITH ADP; HYDROGENCARBONATE; BIOTIN AND MAGNESIUM, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, AND MUTAGENESIS OF
RP GLU-296 AND ARG-338.
RX PubMed=19213731; DOI=10.1074/jbc.m805783200;
RA Chou C.Y., Yu L.P., Tong L.;
RT "Crystal structure of biotin carboxylase in complex with substrates and
RT implications for its catalytic mechanism.";
RL J. Biol. Chem. 284:11690-11697(2009).
CC -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC carboxylase complex; first, biotin carboxylase catalyzes the
CC carboxylation of the carrier protein and then the transcarboxylase
CC transfers the carboxyl group to form malonyl-CoA.
CC {ECO:0000305|PubMed:16793549, ECO:0000305|PubMed:19213731}.
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:0000269|PubMed:16793549, ECO:0000269|PubMed:19213731};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00409};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=115 uM for ATP (at pH 8) {ECO:0000269|PubMed:16793549};
CC KM=16.2 mM for hydrogencarbonate (at pH 8)
CC {ECO:0000269|PubMed:19213731};
CC KM=35.1 mM for biotin (at pH 8) {ECO:0000269|PubMed:19213731};
CC Note=kcat is 0.228 sec(-1) with ATP as substrate (at pH 8)
CC (PubMed:16793549). kcat is 0.44 sec(-1) with hydrogencarbonate as
CC substrate (at pH 8) (PubMed:19213731). kcat is 0.58 sec(-1) with
CC biotin as substrate (at pH 8) (PubMed:19213731).
CC {ECO:0000269|PubMed:16793549, ECO:0000269|PubMed:19213731};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000305|PubMed:16793549,
CC ECO:0000305|PubMed:19213731}.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl
CC carrier protein, biotin carboxylase and the two subunits of carboxyl
CC transferase in a 2:2 complex. {ECO:0000269|PubMed:10821865,
CC ECO:0000269|PubMed:16793549}.
CC -!- INTERACTION:
CC P24182; P0ABD8: accB; NbExp=10; IntAct=EBI-542308, EBI-542320;
CC P24182; P0A9Q5: accD; NbExp=4; IntAct=EBI-542308, EBI-542064;
CC P24182; P16703: cysM; NbExp=3; IntAct=EBI-542308, EBI-542376;
CC P24182; P25539: ribD; NbExp=3; IntAct=EBI-542308, EBI-552457;
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DR EMBL; M79446; AAA23748.1; -; Genomic_DNA.
DR EMBL; M80458; AAA23409.1; -; Genomic_DNA.
DR EMBL; M83198; AAA23746.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58059.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76288.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77297.1; -; Genomic_DNA.
DR EMBL; M32214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JS0632; JS0632.
DR RefSeq; NP_417722.1; NC_000913.3.
DR RefSeq; WP_000884639.1; NZ_STEB01000012.1.
DR PDB; 1BNC; X-ray; 2.40 A; A/B=1-449.
DR PDB; 1DV1; X-ray; 1.90 A; A/B=1-449.
DR PDB; 1DV2; X-ray; 2.50 A; A/B=1-449.
DR PDB; 2GPS; X-ray; 2.80 A; A/B=1-449.
DR PDB; 2GPW; X-ray; 2.20 A; A/B/C/D=1-449.
DR PDB; 2J9G; X-ray; 2.05 A; A/B=1-449.
DR PDB; 2V58; X-ray; 2.10 A; A/B=1-449.
DR PDB; 2V59; X-ray; 2.40 A; A/B=1-449.
DR PDB; 2V5A; X-ray; 2.31 A; A/B=1-449.
DR PDB; 2VR1; X-ray; 2.60 A; A/B=1-449.
DR PDB; 2W6M; X-ray; 2.00 A; A/B=1-449.
DR PDB; 2W6N; X-ray; 1.87 A; A/B=1-449.
DR PDB; 2W6O; X-ray; 2.50 A; A/C=1-449.
DR PDB; 2W6P; X-ray; 1.85 A; A/B=1-449.
DR PDB; 2W6Q; X-ray; 2.05 A; A/B=1-449.
DR PDB; 2W6Z; X-ray; 1.90 A; A/B=1-449.
DR PDB; 2W70; X-ray; 1.77 A; A/B=1-449.
DR PDB; 2W71; X-ray; 1.99 A; A/C=1-449.
DR PDB; 3G8C; X-ray; 2.00 A; A/B=1-444.
DR PDB; 3G8D; X-ray; 1.90 A; A/B=1-444.
DR PDB; 3JZF; X-ray; 2.13 A; A/B=1-449.
DR PDB; 3JZI; X-ray; 2.31 A; A/B=1-449.
DR PDB; 3RUP; X-ray; 1.99 A; A/B=1-449.
DR PDB; 3RV3; X-ray; 1.91 A; A/B=1-449.
DR PDB; 3RV4; X-ray; 1.98 A; A=1-449.
DR PDB; 4HR7; X-ray; 2.50 A; A/C/E/F=1-449.
DR PDB; 6OI9; X-ray; 2.06 A; A/B=1-449.
DR PDBsum; 1BNC; -.
DR PDBsum; 1DV1; -.
DR PDBsum; 1DV2; -.
DR PDBsum; 2GPS; -.
DR PDBsum; 2GPW; -.
DR PDBsum; 2J9G; -.
DR PDBsum; 2V58; -.
DR PDBsum; 2V59; -.
DR PDBsum; 2V5A; -.
DR PDBsum; 2VR1; -.
DR PDBsum; 2W6M; -.
DR PDBsum; 2W6N; -.
DR PDBsum; 2W6O; -.
DR PDBsum; 2W6P; -.
DR PDBsum; 2W6Q; -.
DR PDBsum; 2W6Z; -.
DR PDBsum; 2W70; -.
DR PDBsum; 2W71; -.
DR PDBsum; 3G8C; -.
DR PDBsum; 3G8D; -.
DR PDBsum; 3JZF; -.
DR PDBsum; 3JZI; -.
DR PDBsum; 3RUP; -.
DR PDBsum; 3RV3; -.
DR PDBsum; 3RV4; -.
DR PDBsum; 4HR7; -.
DR PDBsum; 6OI9; -.
DR AlphaFoldDB; P24182; -.
DR SMR; P24182; -.
DR BioGRID; 4262456; 269.
DR BioGRID; 852073; 6.
DR ComplexPortal; CPX-3206; Acetyl-CoA carboxylase complex.
DR DIP; DIP-9035N; -.
DR IntAct; P24182; 20.
DR STRING; 511145.b3256; -.
DR BindingDB; P24182; -.
DR DrugBank; DB08314; (2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE.
DR DrugBank; DB08315; 2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE.
DR DrugBank; DB08074; 3-(3-Methyl-2-buten-1-yl)-3H-purin-6-amine.
DR DrugBank; DB08075; 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine.
DR DrugBank; DB08076; 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine.
DR DrugBank; DB08316; 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one.
DR DrugBank; DB08317; 5-methyl-6-phenylquinazoline-2,4-diamine.
DR DrugBank; DB08144; 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine.
DR DrugBank; DB08145; 6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE.
DR DrugBank; DB08318; 6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine.
DR DrugBank; DB08146; 7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine.
DR jPOST; P24182; -.
DR PaxDb; P24182; -.
DR PRIDE; P24182; -.
DR EnsemblBacteria; AAC76288; AAC76288; b3256.
DR EnsemblBacteria; BAE77297; BAE77297; BAE77297.
DR GeneID; 58460262; -.
DR GeneID; 947761; -.
DR KEGG; ecj:JW3224; -.
DR KEGG; eco:b3256; -.
DR PATRIC; fig|511145.12.peg.3355; -.
DR EchoBASE; EB0272; -.
DR eggNOG; COG0439; Bacteria.
DR HOGENOM; CLU_000395_3_2_6; -.
DR InParanoid; P24182; -.
DR OMA; FVEICSH; -.
DR PhylomeDB; P24182; -.
DR BioCyc; EcoCyc:BIOTIN-CARBOXYL-MON; -.
DR BioCyc; MetaCyc:BIOTIN-CARBOXYL-MON; -.
DR BRENDA; 6.3.4.14; 2026.
DR SABIO-RK; P24182; -.
DR UniPathway; UPA00655; UER00711.
DR EvolutionaryTrace; P24182; -.
DR PRO; PR:P24182; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IDA:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IC:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004075; F:biotin carboxylase activity; IDA:EcoliWiki.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:ComplexPortal.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IMP:EcoliWiki.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR00514; accC; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Biotin; Direct protein sequencing;
KW Fatty acid biosynthesis; Fatty acid metabolism; Ligase; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..449
FT /note="Biotin carboxylase"
FT /id="PRO_0000146791"
FT DOMAIN 1..445
FT /note="Biotin carboxylation"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT ACT_SITE 292
FT /evidence="ECO:0000269|PubMed:19213731"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:10821865,
FT ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2,
FT ECO:0007744|PDB:3G8D"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:19213731,
FT ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D"
FT BINDING 165..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:10821865,
FT ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2,
FT ECO:0007744|PDB:3G8D"
FT BINDING 201..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:10821865,
FT ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2,
FT ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D"
FT BINDING 209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:19213731,
FT ECO:0007744|PDB:3G8C"
FT BINDING 236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:10821865,
FT ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2,
FT ECO:0007744|PDB:3G8C"
FT BINDING 238
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000269|PubMed:19213731,
FT ECO:0007744|PDB:3G8C"
FT BINDING 276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:19213731,
FT ECO:0007744|PDB:3G8C"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19213731,
FT ECO:0007744|PDB:3G8C"
FT BINDING 276
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:10821865,
FT ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2,
FT ECO:0007744|PDB:3G8D"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19213731,
FT ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 288
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 288
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 290
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 292
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000269|PubMed:19213731,
FT ECO:0007744|PDB:3G8C"
FT BINDING 295
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000269|PubMed:19213731,
FT ECO:0007744|PDB:3G8C"
FT BINDING 338
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000269|PubMed:19213731,
FT ECO:0007744|PDB:3G8C"
FT BINDING 338
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000269|PubMed:19213731,
FT ECO:0007744|PDB:3G8C"
FT MUTAGEN 19
FT /note="R->E: Loss of homodimerization. No effect on ATP
FT binding."
FT /evidence="ECO:0000269|PubMed:16793549"
FT MUTAGEN 23
FT /note="E->R: Loss of homodimerization. No effect on ATP
FT binding."
FT /evidence="ECO:0000269|PubMed:16793549"
FT MUTAGEN 296
FT /note="E->A: Severe reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:19213731"
FT MUTAGEN 338
FT /note="R->A: Severe reduction in catalytic activity."
FT /evidence="ECO:0000269|PubMed:19213731"
FT MUTAGEN 363
FT /note="F->A: Loss of homodimerization. No effect on ATP
FT binding."
FT /evidence="ECO:0000269|PubMed:16793549"
FT MUTAGEN 366
FT /note="R->E: Loss of homodimerization. No effect on ATP
FT binding."
FT /evidence="ECO:0000269|PubMed:16793549"
FT CONFLICT 136
FT /note="G -> A (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="A -> P (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 260..261
FT /note="CA -> SR (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="L -> M (in Ref. 1; AAA23748)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:2W70"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:2W70"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:2W70"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:2W70"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:2W70"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:2W70"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2W70"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:2W70"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:2W70"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:2W70"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:2W70"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:2W70"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:2W70"
FT HELIX 107..114
FT /evidence="ECO:0007829|PDB:2W70"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:2W70"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:2W70"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:2W70"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:2W70"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:2W70"
FT HELIX 175..193
FT /evidence="ECO:0007829|PDB:2W70"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:2W70"
FT STRAND 208..216
FT /evidence="ECO:0007829|PDB:2W70"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:2W6O"
FT STRAND 222..234
FT /evidence="ECO:0007829|PDB:2W70"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:2W70"
FT HELIX 250..267
FT /evidence="ECO:0007829|PDB:2W70"
FT STRAND 271..280
FT /evidence="ECO:0007829|PDB:2W70"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:2W70"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:2W70"
FT HELIX 308..317
FT /evidence="ECO:0007829|PDB:2W70"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:2W70"
FT STRAND 332..340
FT /evidence="ECO:0007829|PDB:2W70"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:2W70"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:2W70"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:2W70"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:2W70"
FT STRAND 383..394
FT /evidence="ECO:0007829|PDB:2W70"
FT HELIX 395..408
FT /evidence="ECO:0007829|PDB:2W70"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:2W70"
FT HELIX 418..425
FT /evidence="ECO:0007829|PDB:2W70"
FT HELIX 428..432
FT /evidence="ECO:0007829|PDB:2W70"
FT HELIX 439..444
FT /evidence="ECO:0007829|PDB:2W70"
SQ SEQUENCE 449 AA; 49321 MW; 68C55F10ACB4F170 CRC64;
MLDKIVIANR GEIALRILRA CKELGIKTVA VHSSADRDLK HVLLADETVC IGPAPSVKSY
LNIPAIISAA EITGAVAIHP GYGFLSENAN FAEQVERSGF IFIGPKAETI RLMGDKVSAI
AAMKKAGVPC VPGSDGPLGD DMDKNRAIAK RIGYPVIIKA SGGGGGRGMR VVRGDAELAQ
SISMTRAEAK AAFSNDMVYM EKYLENPRHV EIQVLADGQG NAIYLAERDC SMQRRHQKVV
EEAPAPGITP ELRRYIGERC AKACVDIGYR GAGTFEFLFE NGEFYFIEMN TRIQVEHPVT
EMITGVDLIK EQLRIAAGQP LSIKQEEVHV RGHAVECRIN AEDPNTFLPS PGKITRFHAP
GGFGVRWESH IYAGYTVPPY YDSMIGKLIC YGENRDVAIA RMKNALQELI IDGIKTNVDL
QIRIMNDENF QHGGTNIHYL EKKLGLQEK
