ID   C7DY60_BARHN            Unreviewed;       318 AA.
AC   C7DY60;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JUN-2015, entry version 29.
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, ECO:0000256|SAAS:SAAS00057486};
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.
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   ProteinModelPortal; C7DY60; -.
DR   STRING; 283166.BH16340; -.
DR   EnsemblBacteria; CDO40965; CDO40965; PRJBM_01621.
DR   EnsemblBacteria; CDO47661; CDO47661; BM1374165_01689.
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
//