ID C7C063_HELPB Unreviewed; 312 AA.
AC C7C063;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00823};
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};
GN Name=accA {ECO:0000256|HAMAP-Rule:MF_00823,
GN ECO:0000313|EMBL:CAX29346.1};
GN OrderedLocusNames=HELPY_0819 {ECO:0000313|EMBL:CAX29346.1};
OS Helicobacter pylori (strain B38).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=592205 {ECO:0000313|EMBL:CAX29346.1, ECO:0000313|Proteomes:UP000000313};
RN [1] {ECO:0000313|EMBL:CAX29346.1, ECO:0000313|Proteomes:UP000000313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B38 {ECO:0000313|EMBL:CAX29346.1,
RC ECO:0000313|Proteomes:UP000000313};
RX PubMed=20537153; DOI=10.1186/1471-2164-11-368;
RA Thiberge J.M., Boursaux-Eude C., Lehours P., Dillies M.A., Creno S.,
RA Coppee J.Y., Rouy Z., Lajus A., Ma L., Burucoa C., Ruskone-Foumestraux A.,
RA Courillon-Mallet A., De Reuse H., Boneca I.G., Lamarque D., Megraud F.,
RA Delchier J.C., Medigue C., Bouchier C., Labigne A., Raymond J.;
RT "From array-based hybridization of Helicobacter pylori isolates to the
RT complete genome sequence of an isolate associated with MALT lymphoma.";
RL BMC Genomics 11:368-368(2010).
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:0000256|HAMAP-Rule:MF_00823}.
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:0000256|ARBA:ARBA00001072, ECO:0000256|HAMAP-
CC Rule:MF_00823};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956,
CC ECO:0000256|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). {ECO:0000256|HAMAP-Rule:MF_00823}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00823}.
CC -!- SIMILARITY: Belongs to the AccA family. {ECO:0000256|HAMAP-
CC Rule:MF_00823}.
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DR EMBL; FM991728; CAX29346.1; -; Genomic_DNA.
DR RefSeq; WP_001029386.1; NC_012973.1.
DR AlphaFoldDB; C7C063; -.
DR SMR; C7C063; -.
DR KEGG; hpb:HELPY_0819; -.
DR HOGENOM; CLU_015486_0_2_7; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000000313; 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 NCBIfam; TIGR00513; accA; 1.
DR NCBIfam; NF041504; AccA_sub; 1.
DR PANTHER; PTHR42853; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR42853:SF3; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA, CHLOROPLASTIC; 1.
DR Pfam; PF03255; ACCA; 1.
DR PRINTS; PR01069; ACCCTRFRASEA.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00823}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00823};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW Rule:MF_00823};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_00823}; Ligase {ECO:0000313|EMBL:CAX29346.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00823};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00823};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00823};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00823}.
FT DOMAIN 36..286
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 312 AA; 34909 MW; CC05B47663866D81 CRC64;
MAIYLDFENH IKEIQNEIEL ALIRGDEDAK EILEKRLDKE VKSIYSNLTD FQKLQLARHP
DRPYAMDYID LILKDKYEVF GDRHYNDDKA IVCFIGKIDN VPVVVIGEEK GRGTKNKLLR
NFGMPNPCGY RKALKMAKFA EKFNLPILML VDTAGAYPGI GAEERGQSEA IAKNLQEFAS
LKVPTISVII GEGGSGGALA IAVADKLAMM EYSIFSVISP EGCAAILWDD PSKTEVAIKA
MKITPRDLKE AGLIDDIILE PSKGAHRDKF SAANTIKEYF LDALRTIQQD PHFLDNRYQK
LMSLGSFVES MN
//
