ID C9RBG3_AMMDK Unreviewed; 323 AA.
AC C9RBG3;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 79.
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 OrderedLocusNames=Adeg_0438 {ECO:0000313|EMBL:ACX51590.1};
OS Ammonifex degensii (strain DSM 10501 / KC4).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Ammonifex.
OX NCBI_TaxID=429009 {ECO:0000313|EMBL:ACX51590.1, ECO:0000313|Proteomes:UP000002620};
RN [1] {ECO:0000313|EMBL:ACX51590.1, ECO:0000313|Proteomes:UP000002620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10501 / KC4 {ECO:0000313|Proteomes:UP000002620};
RG US DOE Joint Genome Institute;
RA Kerfeld C., Goodner B., Huber H., Stetter K., Lucas S., Copeland A.,
RA Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Ovchinnikova G., Richardson P.;
RT "Complete sequence of chromosome of Ammonifex degensii KC4.";
RL Submitted (OCT-2009) 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; CP001785; ACX51590.1; -; Genomic_DNA.
DR RefSeq; WP_015738468.1; NC_013385.1.
DR AlphaFoldDB; C9RBG3; -.
DR STRING; 429009.Adeg_0438; -.
DR KEGG; adg:Adeg_0438; -.
DR eggNOG; COG0825; Bacteria.
DR HOGENOM; CLU_015486_0_2_9; -.
DR OrthoDB; 9808023at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000002620; Chromosome.
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}; Ligase {ECO:0000313|EMBL:ACX51590.1};
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:UP000002620};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00823}.
FT DOMAIN 35..292
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 323 AA; 36095 MW; 06310FDF5995FE37 CRC64;
MPTYLDFERP LVELEEKIAE LTSFSQEKGL DLSEEIAKLH QRAEELKRQI FAHLTPWQKV
QLARHPDRPT TLDYIRLLCE EFTELHGDRL YGDDPAIVGG IAWFAGRPVM VLGHQKGKDT
RENMRRNFGM PHPEGFRKAL RLMLQAEKFG RPIITFIDTP GAYCGIGAEE RGQSVAIAQN
LARMSSLRVP IIVVVIGEGG SGGALALAVG DRILMQEHAI FSVISPEGCA SILWKDASRA
KEAAEALKLT AQDLLALGLI DEVIPEPLGG AHRNREGAAE FLREALLRHL EELEGIPPDE
LCRQRYAKYR RVGPTFYQGE REA
//
