ID C7DY60_BARHN Unreviewed; 318 AA. AC C7DY60; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 22-JUL-2015, entry version 30. 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=6.4.1.2 {ECO:0000256|HAMAP-Rule:MF_00823}; GN Name=accA {ECO:0000256|HAMAP-Rule:MF_00823, GN ECO:0000313|EMBL:ACT33034.1}; GN ORFNames=BM1374165_01689 {ECO:0000313|EMBL:CDO47661.1}; OS Bartonella henselae (Rochalimaea henselae). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=38323 {ECO:0000313|EMBL:ACT33034.1}; RN [1] {ECO:0000313|EMBL:ACT33036.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JK40 {ECO:0000313|EMBL:ACT33036.1}; RA Hsu Y.-M., Chan Y.-J., Chang C.-C.; RT "Acetyl-CoA carboxylase carboxyltransferase subunit alpha gene of RT Bartonella henselae JK40 strain."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACT33035.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JK47 {ECO:0000313|EMBL:ACT33035.1}; RA Hsu Y.-M., Chan Y.-J., Chang C.-C.; RT "Acetyl-CoA carboxylase carboxyltransferase subunit alpha gene of RT Bartonella henselae JK47 strain."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ACT33034.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=U4 {ECO:0000313|EMBL:ACT33034.1}; RA Hsu Y.-M., Chan Y.-J., Chang C.-C.; RT "Acetyl-CoA carboxylase carboxyltransferase subunit alpha gene of RT Bartonella henselae U4 strain."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|Proteomes:UP000019801} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BM1374165 {ECO:0000313|Proteomes:UP000019801}; RA Raoult D.; RT "Genome sequencing of Bartonella spp. isolated from human blood."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:CDO47661.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BM1374165 {ECO:0000313|EMBL:CDO47661.1}; RA GENOMES U.; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:CDO47661.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BM1374165 {ECO:0000313|EMBL:CDO47661.1}; RA Raoult D.; RT "Genome sequencing of Bartonella spp. isolated from human blood."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. 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: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate CC + malonyl-CoA. {ECO:0000256|HAMAP-Rule:MF_00823, CC ECO:0000256|SAAS:SAAS00057344}. 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:SAAS00177030}. 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; GQ227672; ACT33034.1; -; Genomic_DNA. DR EMBL; GQ227673; ACT33035.1; -; Genomic_DNA. DR EMBL; GQ227674; ACT33036.1; -; Genomic_DNA. DR EMBL; HG969191; CDO47661.1; -; Genomic_DNA. DR RefSeq; WP_011181396.1; NZ_HG969191.1. DR STRING; 283166.BH16340; -. DR EnsemblBacteria; CDO40965; CDO40965; PRJBM_01621. DR EnsemblBacteria; CDO47661; CDO47661; BM1374165_01689. DR KEGG; bhn:PRJBM_01621; -. DR KEGG; bhs:BM1374165_01689; -. DR KO; K01962; -. DR UniPathway; UPA00655; UER00711. DR Proteomes; UP000019801; Chromosome. DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.90.226.10; -; 1. DR HAMAP; MF_00823; AcetylCoA_CT_alpha; 1. DR InterPro; IPR001095; Acetyl_CoA_COase_a_su. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR011763; COA_CT_C. 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|HAMAP-Rule:MF_00823, KW ECO:0000256|SAAS:SAAS00057445}; KW Complete proteome {ECO:0000313|Proteomes:UP000019801}; 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:SAAS00057508}; KW Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_00823, KW ECO:0000256|SAAS:SAAS00057516}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00823, KW ECO:0000256|SAAS:SAAS00057419}; KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00823, KW ECO:0000256|SAAS:SAAS00057490}; KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00823, KW ECO:0000256|SAAS:SAAS00057497}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00823, KW ECO:0000256|SAAS:SAAS00057352}; KW Transferase {ECO:0000313|EMBL:ACT33034.1}. SQ SEQUENCE 318 AA; 34949 MW; 6C00D9F41B171DD4 CRC64; MYNYLDFEKP VADLDGKILE LKKISQEEGS LDMSDEIARL EMRSKTALRD IYKKLSPWQK TQVARHPDRP HFMDYSARLL SDVTPLAGDR KFAEDEAIQA GFARFKGEAV AYIGQEKGHD TQTRLRYNFG SARPEGYRKA VRIMEMADRF GLPLLTFVDT AGAYPGVSAE ERGQAEAIAQ STAATLRLKV PVVSVVIGEG GSGGAIAIAA ANKVYMLEHA IYSVISPEGA ASILWRDPTR AKDAAMNMRI TAQDLYQLKI IDGIIPEPLG GAHRGKEAVI DATGDIISFA LEAMAGKEGD VLKQERREKY LQIGRSLA //