ID A0A7G4RP39_XYLFS Unreviewed; 319 AA. AC A0A7G4RP39; DT 10-FEB-2021, integrated into UniProtKB/TrEMBL. DT 10-FEB-2021, sequence version 1. DT 07-APR-2021, entry version 2. 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 ORFNames=XFGV230_00810 {ECO:0000313|EMBL:QNH30772.1}; OS Xylella fastidiosa subsp. fastidiosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=644356 {ECO:0000313|EMBL:QNH30772.1}; RN [1] {ECO:0000313|EMBL:QNH30772.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GV230 {ECO:0000313|EMBL:QNH30772.1}; RA Weng L.-W., Lin Y.-C., Cho S.-T., Tsai Y.-M., Su C.-C., Tsai C.-W., RA Kuo C.-H.; RT "Complete genome sequence of Xylella fastidiosa subsp. fastidiosa GV230."; RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP060159; QNH30772.1; -; Genomic_DNA. DR RefSeq; WP_004572984.1; NZ_VOSD01000001.1. DR GeneID; 58015721; -. DR UniPathway; UPA00655; UER00711. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC. 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 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; 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:QNH30772.1}; 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 32..293 FT /note="CoA carboxyltransferase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS50989" SQ SEQUENCE 319 AA; 35631 MW; 87B4AEF89620B65C CRC64; MNPNYLDFEQ PIADLEAKIQ DLRTASAGPS VNVDIEVRAL ENKLRLRTAQ IFRNLSAWQI SQLARHPRRP YTLDYISIVC DEFQELAGDR TLADDKAIVG GLARIGHRPV MLIGHQKGRD NKERLMRNFG MPKPEGYRKA LRLMKLAERF GLPLLTFIDT MGAWPGIDAE ERNQSEAIAT NLIEMAELKI PVICTVIGEG GSGGALAIGI GDRTLMLEYS TYSVITPEGC ASILWKDAAK ASDAAEQLNL TARRLKEFGL IDKVIREPIG GAHRNPQQMA NRLKAVLLNE LEALDKVPLV TLLNQRHKRL RTYGAYENH //