ID W3AR72_9FIRM Unreviewed; 449 AA.
AC W3AR72;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Biotin carboxylase {ECO:0000256|RuleBase:RU365063};
DE EC=6.3.4.14 {ECO:0000256|RuleBase:RU365063};
DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000256|RuleBase:RU365063};
GN ORFNames=UYO_0428 {ECO:0000313|EMBL:ETP73491.1};
OS Lachnospiraceae bacterium JC7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1165092 {ECO:0000313|EMBL:ETP73491.1, ECO:0000313|Proteomes:UP000018967};
RN [1] {ECO:0000313|EMBL:ETP73491.1, ECO:0000313|Proteomes:UP000018967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC7 {ECO:0000313|EMBL:ETP73491.1,
RC ECO:0000313|Proteomes:UP000018967};
RA Rosewarne C.P., Cheung J.L., Evans P.N., Tomkins N.W., Denman S.E.,
RA O Cuiv P., Morrison M.;
RT "Isolation and genomic characterisation of Lachnospiraceae sp. JC7, a newly
RT identified member of the bovine rumen core microbiota.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
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|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|RuleBase:RU365063};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {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|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:ETP73491.1}.
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DR EMBL; ALYD01000003; ETP73491.1; -; Genomic_DNA.
DR AlphaFoldDB; W3AR72; -.
DR PATRIC; fig|1165092.3.peg.429; -.
DR OrthoDB; 9807469at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000018967; 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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
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; IPR013815; ATP_grasp_subdomain_1.
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; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 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; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Biotin {ECO:0000256|ARBA:ARBA00023267, 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..446
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 449 AA; 49467 MW; 92659E2806425C17 CRC64;
MFKRVLVANR GEIAVRVIRA LRDMGIVSVA VYSKEDRDAL HVRLADLRVC IGEGPARDSY
LNMDAIISAA LNMECEAIHP GYGFLSENSE FARRCEENNL EFIGPAYWII DEMGNKSAAR
KKMMEAGVPV VPGTKEPVYD SAAALVEARN IGFPVMIKAS SGGGGKGMRE CFSEDDFEDA
FNTAQRESAN AFGDDTMYIE KLVVHPRHVE VQLIGDKFGN IVTLGERDCS VQRNHQKLIE
ESPSPAIDQE TRSKMYHDAA LAAQTVGYNS AGTIEFIVDQ SGEYYFMEMN TRIQVEHGVT
EMETGTDLMV EQIRVAAGEK LSFTQEDIVL KGHTIECRVN AEIPEKHFMP SPGKITNLLL
PGGNGVRVDT AVYTGYTIPS EYDSMIAKII VHAPTREAAI MKMKAALDET VIMGVDTNLD
FQYKIMNNLT FVSGKADTGF IAAFTEGGR
//
