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Entry: A0A1I0E8K7_9FIRM
LinkDB: A0A1I0E8K7_9FIRM
Original site: A0A1I0E8K7_9FIRM 
ID   A0A1I0E8K7_9FIRM        Unreviewed;       310 AA.
AC   A0A1I0E8K7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=SAMN04487771_101712 {ECO:0000313|EMBL:SET41192.1};
OS   [Clostridium] aminophilum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1526 {ECO:0000313|EMBL:SET41192.1, ECO:0000313|Proteomes:UP000199820};
RN   [1] {ECO:0000313|EMBL:SET41192.1, ECO:0000313|Proteomes:UP000199820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH1P1 {ECO:0000313|EMBL:SET41192.1,
RC   ECO:0000313|Proteomes:UP000199820};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOIL01000017; SET41192.1; -; Genomic_DNA.
DR   RefSeq; WP_074649317.1; NZ_FOIL01000017.1.
DR   AlphaFoldDB; A0A1I0E8K7; -.
DR   STRING; 1526.SAMN02910262_00332; -.
DR   eggNOG; COG0825; Bacteria.
DR   OrthoDB; 9808023at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000199820; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   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:UP000199820};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00823}.
FT   DOMAIN          30..290
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   COILED          277..304
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   310 AA;  34545 MW;  FACC7BB0A9E439DB CRC64;
     MIKEILRQTD EIDAEIEKLR IRREPENSRR TDMRIAQLGE RRNYLLSQAR NLSPEDKVFL
     ARLGARPHID DFIDALFTDF FEQKGDHLYG DDQSIFGGIA RFHGRPVTVL GHRKGRTMKE
     NISRNFGMPK PEGYRKALRM MEQADKFGRP IITFVDTPGA YPGVDAEEHG QGEAIARNLA
     AMSRLRVPVI TVVTGEGNSG GALAISVANR ILMLENAVYS ILSPEGFASI LWKDSSRHAE
     AAALMKMTAA DLKEAGVADE IVAEPAGGAQ VNPLLVYAAL DEAIEKNLKE LEELSSRVLI
     EERQKKFRAM
//
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