(data stored in SCRATCH zone)

SWISSPROT: C8U1Q3_ECO10

ID   C8U1Q3_ECO10            Unreviewed;       319 AA.
AC   C8U1Q3;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00823, ECO:0000256|SAAS:SAAS00176990};
DE            Short=ACCase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00823};
DE            Short=Acetyl-CoA carboxylase carboxyltransferase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00823};
DE            EC=2.1.3.15 {ECO:0000256|HAMAP-Rule:MF_00823, ECO:0000256|SAAS:SAAS01087405};
GN   Name=accA {ECO:0000256|HAMAP-Rule:MF_00823,
GN   ECO:0000313|EMBL:BAI29061.1};
GN   OrderedLocusNames=ECO103_0183 {ECO:0000313|EMBL:BAI29061.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29061.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29061.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC)
CC       complex. First, biotin carboxylase catalyzes the carboxylation of
CC       biotin on its carrier protein (BCCP) and then the CO(2) group is
CC       transferred by the carboxyltransferase to acetyl-CoA to form
CC       malonyl-CoA. {ECO:0000256|HAMAP-Rule:MF_00823,
CC       ECO:0000256|SAAS:SAAS00177034}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] =
CC         malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein];
CC         Xref=Rhea:RHEA:54728, Rhea:RHEA-COMP:10505, Rhea:RHEA-
CC         COMP:10506, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00823,
CC         ECO:0000256|SAAS:SAAS01122170};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00823,
CC       ECO:0000256|SAAS:SAAS00057363}.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of
CC       biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC)
CC       and two subunits each of ACCase subunit alpha (AccA) and ACCase
CC       subunit beta (AccD). {ECO:0000256|HAMAP-Rule:MF_00823,
CC       ECO:0000256|SAAS:SAAS00176983}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00823,
CC       ECO:0000256|SAAS:SAAS00231887}.
CC   -!- SIMILARITY: Belongs to the AccA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00823, ECO:0000256|SAAS:SAAS00588190}.
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DR   EMBL; AP010958; BAI29061.1; -; Genomic_DNA.
DR   RefSeq; WP_000055746.1; NC_013353.1.
DR   SMR; C8U1Q3; -.
DR   EnsemblBacteria; BAI29061; BAI29061; ECO103_0183.
DR   KEGG; eoh:ECO103_0183; -.
DR   HOGENOM; HOG000273832; -.
DR   KO; K01962; -.
DR   OMA; MFEHSVY; -.
DR   BioCyc; ECOL585395:ECO103_RS00935-MONOMER; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
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:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
DR   PRODOM; C8U1Q3.
DR   SWISS-2DPAGE; C8U1Q3.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00823,
KW   ECO:0000256|SAAS:SAAS00127049}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00823,
KW   ECO:0000256|SAAS:SAAS00177046};
KW   Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00823,
KW   ECO:0000256|SAAS:SAAS00126967};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_00823,
KW   ECO:0000256|SAAS:SAAS00127008};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00823,
KW   ECO:0000256|SAAS:SAAS00127050};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00823,
KW   ECO:0000256|SAAS:SAAS00126977};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00823,
KW   ECO:0000256|SAAS:SAAS00057352};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00823,
KW   ECO:0000256|SAAS:SAAS01087435, ECO:0000313|EMBL:BAI29061.1}.
FT   DOMAIN       35    296       CoA carboxyltransferase C-terminal.
FT                                {ECO:0000259|PROSITE:PS50989}.
FT   COILED       12     32       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   319 AA;  35288 MW;  1C1F8DE48D88E946 CRC64;
     MSLNFLDFEQ PIAELEAKID SLTAVSRQDE KLDINIDEEV HRLREKSVEL TRKIFADLGA
     WQIAQLARHP QRPYTLDYVR LAFDEFDELA GDRAYADDKA IVGGIARLDG RPVMIIGHQK
     GRETKEKIRR NFGMPAPEGY RKALRLMQMA ERFKMPIITF IDTPGAYPGV GAEERGQSEA
     IARNLREMSR LSVPTICTVI GEGGSGGALA IGVGDKVNML QYSTYSVISP EGCASILWKS
     ADKAPLAAEA MGIIAPRLKE LKLIDSIIPE PLGGAHRNPE AMAASLKAQL LADLADLDVL
     STEDLKNRRY QRLMSYGYA
//

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