ID A0A0C1K262_9BACT Unreviewed; 454 AA.
AC A0A0C1K262;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Biotin carboxylase {ECO:0000256|ARBA:ARBA00013263, ECO:0000256|RuleBase:RU365063};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263, ECO:0000256|RuleBase:RU365063};
DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000256|RuleBase:RU365063};
GN Name=accC {ECO:0000313|EMBL:KIC76761.1};
GN ORFNames=DB41_EO00140 {ECO:0000313|EMBL:KIC76761.1};
OS Neochlamydia sp. TUME1.
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Neochlamydia.
OX NCBI_TaxID=1478174 {ECO:0000313|EMBL:KIC76761.1, ECO:0000313|Proteomes:UP000031320};
RN [1] {ECO:0000313|EMBL:KIC76761.1, ECO:0000313|Proteomes:UP000031320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUME1 {ECO:0000313|EMBL:KIC76761.1,
RC ECO:0000313|Proteomes:UP000031320};
RX PubMed=25069652; DOI=10.1093/molbev/msu227;
RA Domman D., Collingro A., Lagkouvardos I., Gehre L., Weinmaier T.,
RA Rattei T., Subtil A., Horn M.;
RT "Massive expansion of Ubiquitination-related gene families within the
RT Chlamydiae.";
RL Mol. Biol. Evol. 31:2890-2904(2014).
CC -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC carboxylase complex; first, biotin carboxylase catalyzes the
CC carboxylation of the carrier protein and then the transcarboxylase
CC transfers the carboxyl group to form malonyl-CoA.
CC {ECO:0000256|ARBA:ARBA00003761, ECO:0000256|RuleBase:RU365063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC ChEBI:CHEBI:456216; EC=6.3.4.14;
CC Evidence={ECO:0000256|ARBA:ARBA00000861,
CC ECO:0000256|RuleBase:RU365063};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956,
CC ECO:0000256|RuleBase:RU365063}.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl
CC carrier protein, biotin carboxylase and the two subunits of carboxyl
CC transferase in a 2:2 complex. {ECO:0000256|ARBA:ARBA00011750,
CC ECO:0000256|RuleBase:RU365063}.
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:KIC76761.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JRXI01000054; KIC76761.1; -; Genomic_DNA.
DR RefSeq; WP_039383906.1; NZ_JRXI01000054.1.
DR AlphaFoldDB; A0A0C1K262; -.
DR PATRIC; fig|1478174.3.peg.546; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000031320; Unassembled WGS sequence.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR NCBIfam; TIGR00514; accC; 1.
DR PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|RuleBase:RU365063};
KW Fatty acid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW Fatty acid metabolism {ECO:0000256|RuleBase:RU365063};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU365063};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW Lipid metabolism {ECO:0000256|RuleBase:RU365063};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..445
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 454 AA; 49686 MW; 4BAB040D30AE9F55 CRC64;
MQKVLIANRG EIAVRIIRAC HDLGLQTVAV YSQADAEALH VLHADEAICI GEAPAAKSYL
KISNILSACE ITGADAIHPG YGFLSENANF ASICESCGLN FIGPAPASIT LLGDKAKAKA
TAKKAGCPVI PGSEGIVSDL KEGLEVAKEI GYPIFIKAVS GGGGKGIRIA YSEEEFIRLF
PAARAEADAS FSNPDVYLEK MIVDPRHIEV QVIGDKYGNY IHLGERDCSI QRRRQKLIEE
APSPLLNSKL RQKIGQAAIN VVKEANYHSV ATVEFLLDAD HHFYFMEVNT RIQVEHTVTE
ELTGVDLLGE QLSVAMGNKL RYAQEEINFK GHVIQFRINA ENPAANFSPS PGRLEYYLPP
GGPHVRVDSA CYSGYQIPPN YDSMIAKLIV HGKDRLEAIA IGKRALREFH IGGVDSTIPF
HLYMLHDKKF LHSDFHLSYI DGLIAEGCSF SLEE
//
