ID A0A1D8URM6_9PROT Unreviewed; 318 AA.
AC A0A1D8URM6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
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:GEL63646.1};
GN ORFNames=A0U89_03240 {ECO:0000313|EMBL:AOX16299.1}, KBA01_09320
GN {ECO:0000313|EMBL:GEL63646.1};
OS Kozakia baliensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Kozakia.
OX NCBI_TaxID=153496 {ECO:0000313|EMBL:AOX16299.1, ECO:0000313|Proteomes:UP000179145};
RN [1] {ECO:0000313|EMBL:AOX16299.1, ECO:0000313|Proteomes:UP000179145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14400 {ECO:0000313|EMBL:AOX16299.1,
RC ECO:0000313|Proteomes:UP000179145};
RX PubMed=27716345;
RA Brandt J.U., Jakob F., Behr J., Geissler A.J., Vogel R.F.;
RT "Dissection of exopolysaccharide biosynthesis in Kozakia baliensis.";
RL Microb. Cell Fact. 15:170-170(2016).
RN [2] {ECO:0000313|EMBL:AOX16299.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 14400 {ECO:0000313|EMBL:AOX16299.1};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:GEL63646.1, ECO:0000313|Proteomes:UP000321177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16664 {ECO:0000313|EMBL:GEL63646.1,
RC ECO:0000313|Proteomes:UP000321177};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Kozakia baliensis NBRC 16664.";
RL Submitted (JUL-2019) 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; CP014674; AOX16299.1; -; Genomic_DNA.
DR EMBL; BJVW01000002; GEL63646.1; -; Genomic_DNA.
DR RefSeq; WP_029604344.1; NZ_JNAB01000018.1.
DR AlphaFoldDB; A0A1D8URM6; -.
DR STRING; 153496.A0U89_03240; -.
DR KEGG; kba:A0U89_03240; -.
DR eggNOG; COG0825; Bacteria.
DR OrthoDB; 9808023at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000179145; Chromosome.
DR Proteomes; UP000321177; 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}; Reference proteome {ECO:0000313|Proteomes:UP000179145};
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; 34511 MW; A60C13E904B09865 CRC64;
MRQYLDFEKP VAELENKIAE LRQMAKDGEG INIADEIGKL SDKSEKQLRA AYAKLTPWQK
VMVARHAQRP QALDYFRDLL TDYTPLAGDR LGHNDQAIVG GMARFRGQPV MVIGTERGFD
MESRLLHNFG MPKPEGYRKA QRFVDLAGRF GLPVLTFIDT SGAWPGIDAE QRGQAQAIAK
STDCFLRAPV PVIATIIGEG GSGGAVALGA GDRVLMLEHS IYSVIAPEGA ASILWRDPKQ
AATAAEALRL TAQDLLKLKL IDRIISEPVG GAQRFPQEAT AAVGEAIAAE LPALIALDPA
ALVSQRREKF LAMGREAL
//
