ID   C7DY60_BARHN            Unreviewed;       318 AA.
AC   C7DY60; A0A0H3M017;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   08-NOV-2023, entry version 73.
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:ACT33034.1};
GN   ORFNames=BH623125_06830 {ECO:0000313|EMBL:GFF02249.1}, BH80429_14760
GN   {ECO:0000313|EMBL:GFF04655.1}, BM1374165_01689
GN   {ECO:0000313|EMBL:CDO47661.1};
OS   Bartonella henselae (Rochalimaea henselae).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
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.
RN   [7] {ECO:0000313|EMBL:GFF02249.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=623-125 {ECO:0000313|EMBL:GFF02249.1}, and 804-29
RC   {ECO:0000313|EMBL:GFF04655.1};
RA   Tsukamoto K., Shinzawa N., Kawai A., Suzuki M., Kidoya H., Takakura N.,
RA   Yamaguchi H., Kameyama T., Inagaki H., Kurahashi H., Horiguchi Y., Doi Y.;
RT   "The Bartonella autotransporter BafA activates the host VEGF pathway to
RT   drive angiogenesis.";
RL   Nat. Commun. 11:0-3571(2020).
RN   [8] {ECO:0000313|Proteomes:UP000503821, ECO:0000313|Proteomes:UP000503841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=623-125 {ECO:0000313|Proteomes:UP000503841}, and 804-29
RC   {ECO:0000313|Proteomes:UP000503821};
RA   Tsukamoto K., Shinzawa N., Kawai A., Suzuki M., Horiguchi Y., Kidoya H.,
RA   Takakura N., Kameyama T., Inagaki H., Kurahashi H., Doi Y.;
RT   "Bartonella autotransporter BafA induces angiogenesis via VEGFR2-ERK
RT   signaling.";
RL   Submitted (JAN-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}.
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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   EMBL; BLJS01000001; GFF02249.1; -; Genomic_DNA.
DR   EMBL; BLJT01000001; GFF04655.1; -; Genomic_DNA.
DR   RefSeq; WP_011181396.1; NZ_LOAI01000011.1.
DR   AlphaFoldDB; C7DY60; -.
DR   STRING; 38323.BM1374165_01689; -.
DR   EnsemblBacteria; CDO47661; CDO47661; BM1374165_01689.
DR   GeneID; 64157770; -.
DR   KEGG; bhn:PRJBM_01621; -.
DR   KEGG; bhs:BM1374165_01689; -.
DR   PATRIC; fig|38323.3.peg.1882; -.
DR   OMA; TPWQRVQ; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000019801; Chromosome.
DR   Proteomes; UP000503821; Unassembled WGS sequence.
DR   Proteomes; UP000503841; Unassembled WGS sequence.
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};
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          40..293
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
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
//