ACCA_ECOLI
ID ACCA_ECOLI Reviewed; 319 AA.
AC P0ABD5; P30867;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823};
DE Short=ACCase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823};
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823};
DE EC=2.1.3.15 {ECO:0000255|HAMAP-Rule:MF_00823, ECO:0000269|PubMed:15066985};
GN Name=accA {ECO:0000255|HAMAP-Rule:MF_00823};
GN OrderedLocusNames=b0185, JW0180;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=1355089; DOI=10.1016/s0021-9258(18)41860-1;
RA Li S.-J., Cronan J.E. Jr.;
RT "The genes encoding the two carboxyltransferase subunits of Escherichia
RT coli acetyl-CoA carboxylase.";
RL J. Biol. Chem. 267:16841-16847(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9339543; DOI=10.1266/ggs.72.167;
RA Yamamoto Y., Miwa Y., Miyoshi K., Furuyama J., Ohmori H.;
RT "The Escherichia coli ldcC gene encodes another lysine decarboxylase,
RT probably a constitutive enzyme.";
RL Genes Genet. Syst. 72:167-172(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 24.
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-319.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9226257; DOI=10.1128/jb.179.14.4486-4492.1997;
RA Kikuchi Y., Kojima H., Tanaka T., Takatsuka Y., Kamio Y.;
RT "Characterization of a second lysine decarboxylase isolated from
RT Escherichia coli.";
RL J. Bacteriol. 179:4486-4492(1997).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RX PubMed=3316192; DOI=10.1128/jb.169.12.5735-5744.1987;
RA Tomasiewicz H.G., McHenry C.S.;
RT "Sequence analysis of the Escherichia coli dnaE gene.";
RL J. Bacteriol. 169:5735-5744(1987).
RN [9]
RP PROTEIN SEQUENCE OF 2-13.
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 [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=15066985; DOI=10.1074/jbc.m402989200;
RA Freiberg C., Brunner N.A., Schiffer G., Lampe T., Pohlmann J., Brands M.,
RA Raabe M., Haebich D., Ziegelbauer K.;
RT "Identification and characterization of the first class of potent bacterial
RT acetyl-CoA carboxylase inhibitors with antibacterial activity.";
RL J. Biol. Chem. 279:26066-26073(2004).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RX PubMed=16460018; DOI=10.1021/bi0520479;
RA Bilder P., Lightle S., Bainbridge G., Ohren J., Finzel B., Sun F.,
RA Holley S., Al-Kassim L., Spessard C., Melnick M., Newcomer M.,
RA Waldrop G.L.;
RT "The structure of the carboxyltransferase component of acetyl-coA
RT carboxylase reveals a zinc-binding motif unique to the bacterial enzyme.";
RL Biochemistry 45:1712-1722(2006).
CC -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex.
CC First, biotin carboxylase catalyzes the carboxylation of biotin on its
CC carrier protein (BCCP) and then the CO(2) group is transferred by the
CC carboxyltransferase to acetyl-CoA to form malonyl-CoA.
CC {ECO:0000255|HAMAP-Rule:MF_00823, ECO:0000269|PubMed:15066985}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-
CC CoA + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54728,
CC Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00823,
CC ECO:0000269|PubMed:15066985};
CC -!- ACTIVITY REGULATION: Competitively inhibited by pyrrolidine dione
CC antibiotic moiramide B (CPD1). {ECO:0000269|PubMed:15066985}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=100 uM for malonyl-CoA {ECO:0000269|PubMed:15066985};
CC KM=10 mM for biocytin {ECO:0000269|PubMed:15066985};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00823}.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two
CC subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta
CC (AccD).
CC -!- INTERACTION:
CC P0ABD5; P0ABD5: accA; NbExp=2; IntAct=EBI-542031, EBI-542031;
CC P0ABD5; P0A9Q5: accD; NbExp=17; IntAct=EBI-542031, EBI-542064;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the AccA family. {ECO:0000255|HAMAP-
CC Rule:MF_00823}.
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DR EMBL; M96394; AAA70370.1; -; Genomic_DNA.
DR EMBL; D49445; BAA08425.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08614.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73296.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77860.2; -; Genomic_DNA.
DR EMBL; D87518; BAA21655.1; -; Genomic_DNA.
DR EMBL; M19334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A43452; A43452.
DR RefSeq; NP_414727.1; NC_000913.3.
DR RefSeq; WP_000055741.1; NZ_STEB01000032.1.
DR PDB; 2F9Y; X-ray; 3.20 A; A=1-319.
DR PDBsum; 2F9Y; -.
DR AlphaFoldDB; P0ABD5; -.
DR SMR; P0ABD5; -.
DR BioGRID; 4259753; 211.
DR BioGRID; 849295; 5.
DR ComplexPortal; CPX-3206; Acetyl-CoA carboxylase complex.
DR DIP; DIP-35897N; -.
DR IntAct; P0ABD5; 32.
DR MINT; P0ABD5; -.
DR STRING; 511145.b0185; -.
DR jPOST; P0ABD5; -.
DR PaxDb; P0ABD5; -.
DR PRIDE; P0ABD5; -.
DR EnsemblBacteria; AAC73296; AAC73296; b0185.
DR EnsemblBacteria; BAA77860; BAA77860; BAA77860.
DR GeneID; 66671527; -.
DR GeneID; 944895; -.
DR KEGG; ecj:JW0180; -.
DR KEGG; eco:b0185; -.
DR PATRIC; fig|1411691.4.peg.2094; -.
DR EchoBASE; EB1600; -.
DR eggNOG; COG0825; Bacteria.
DR HOGENOM; CLU_015486_0_2_6; -.
DR InParanoid; P0ABD5; -.
DR OMA; TPWQRVQ; -.
DR PhylomeDB; P0ABD5; -.
DR BioCyc; EcoCyc:CARBOXYL-TRANSFERASE-ALPHA-MON; -.
DR BioCyc; MetaCyc:CARBOXYL-TRANSFERASE-ALPHA-MON; -.
DR BRENDA; 2.1.3.15; 2026.
DR BRENDA; 2.3.2.31; 2681.
DR BRENDA; 6.4.1.2; 2026.
DR SABIO-RK; P0ABD5; -.
DR UniPathway; UPA00655; UER00711.
DR EvolutionaryTrace; P0ABD5; -.
DR PRO; PR:P0ABD5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009329; C:acetate CoA-transferase complex; IDA:EcoCyc.
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:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; NAS:EcoliWiki.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IDA:ComplexPortal.
DR HAMAP; MF_00823; AcetylCoA_CT_alpha; 1.
DR InterPro; IPR001095; Acetyl_CoA_COase_a_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR PANTHER; PTHR42853; PTHR42853; 1.
DR Pfam; PF03255; ACCA; 1.
DR PRINTS; PR01069; ACCCTRFRASEA.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR00513; accA; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..319
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit alpha"
FT /id="PRO_0000146774"
FT DOMAIN 35..296
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT HELIX 10..14
FT /evidence="ECO:0007829|PDB:2F9Y"
FT TURN 15..20
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:2F9Y"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:2F9Y"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:2F9Y"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2F9Y"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:2F9Y"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 137..152
FT /evidence="ECO:0007829|PDB:2F9Y"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 177..189
FT /evidence="ECO:0007829|PDB:2F9Y"
FT STRAND 195..204
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:2F9Y"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:2F9Y"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 244..251
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:2F9Y"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:2F9Y"
FT TURN 294..299
FT /evidence="ECO:0007829|PDB:2F9Y"
FT HELIX 302..315
FT /evidence="ECO:0007829|PDB:2F9Y"
SQ SEQUENCE 319 AA; 35242 MW; A810DE891CEA2B4F CRC64;
MSLNFLDFEQ PIAELEAKID SLTAVSRQDE KLDINIDEEV HRLREKSVEL TRKIFADLGA
WQIAQLARHP QRPYTLDYVR LAFDEFDELA GDRAYADDKA IVGGIARLDG RPVMIIGHQK
GRETKEKIRR NFGMPAPEGY RKALRLMQMA ERFKMPIITF IDTPGAYPGV GAEERGQSEA
IARNLREMSR LGVPVVCTVI GEGGSGGALA IGVGDKVNML QYSTYSVISP EGCASILWKS
ADKAPLAAEA MGIIAPRLKE LKLIDSIIPE PLGGAHRNPE AMAASLKAQL LADLADLDVL
STEDLKNRRY QRLMSYGYA
