(data stored in ACNUC7421 zone)

SWISSPROT: ACCA_SHISS

ID   ACCA_SHISS              Reviewed;         319 AA.
AC   Q3Z5H3;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 92.
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};
GN   Name=accA {ECO:0000255|HAMAP-Rule:MF_00823};
GN   OrderedLocusNames=SSON_0197;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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:0000255|HAMAP-Rule:MF_00823}.
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:0000255|HAMAP-Rule:MF_00823};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00823}.
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:0000255|HAMAP-Rule:MF_00823}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00823}.
CC   -!- SIMILARITY: Belongs to the AccA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00823}.
DR   EMBL; CP000038; AAZ86989.1; -; Genomic_DNA.
DR   SMR; Q3Z5H3; -.
DR   PRIDE; Q3Z5H3; -.
DR   EnsemblBacteria; AAZ86989; AAZ86989; SSON_0197.
DR   KEGG; ssn:SSON_0197; -.
DR   HOGENOM; HOG000273832; -.
DR   KO; K01962; -.
DR   OMA; MFEHSVY; -.
DR   BioCyc; SSON300269:G1GL2-229-MONOMER; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000002529; 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; Q3Z5H3.
DR   SWISS-2DPAGE; Q3Z5H3.
KW   ATP-binding; Complete proteome; Cytoplasm; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    319       Acetyl-coenzyme A carboxylase carboxyl
FT                                transferase subunit alpha.
FT                                /FTId=PRO_0000223824.
FT   DOMAIN       35    296       CoA carboxyltransferase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01137}.
SQ   SEQUENCE   319 AA;  35270 MW;  A810DE97FC043B4F 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 AMAVSLKAQL LADLADLDVL
     STEDLKNRRY QRLMSYGYA
//

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