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Database: UniProt
Entry: A0A0F2NYN0_9FLAO
LinkDB: A0A0F2NYN0_9FLAO
Original site: A0A0F2NYN0_9FLAO 
ID   A0A0F2NYN0_9FLAO        Unreviewed;       319 AA.
AC   A0A0F2NYN0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=VR77_01820 {ECO:0000313|EMBL:KJS07138.1};
OS   Flavobacteriales bacterium BRH_c54.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX   NCBI_TaxID=1629721 {ECO:0000313|EMBL:KJS07138.1, ECO:0000313|Proteomes:UP000033681};
RN   [1] {ECO:0000313|EMBL:KJS07138.1, ECO:0000313|Proteomes:UP000033681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c54 {ECO:0000313|EMBL:KJS07138.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJS07138.1}.
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DR   EMBL; LADZ01000009; KJS07138.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2NYN0; -.
DR   STRING; 1629721.VR77_01820; -.
DR   PATRIC; fig|1629721.3.peg.1290; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000033681; 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          38..293
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   319 AA;  35977 MW;  431774D7EF7FD438 CRC64;
     MPVYLDFEEP IQILEEQLEE HLKLQEEKGV DTSKIVKEIQ KKIKDTRKEL YSNLTPWQRV
     QVSRHPERPY TLAYIKHITD GNFIELHGDR TVKDDKAMVG GFGMIDGQSV MLIGQQKGIN
     TKMRQYRNFG MPNPEGYRKA LRLMKLAEKF NKPVICFVDT PGAFPGLEAE ERGQGEAIAR
     NLFEMAQLQV PIIVVIIGEG ASGGALGIGV GDKVFMMENT WYSVISPESC SSILWRSWDF
     KEQAAAALKL TSTDMLENKL VDGIIKEPVG GAHAAPEEAF DLVKKEILKH LPKLVEMDKD
     KLVEKRINKF CSMGVVVEK
//
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