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Database: UniProt
Entry: F7T063_9BURK
LinkDB: F7T063_9BURK
Original site: F7T063_9BURK 
ID   F7T063_9BURK            Unreviewed;       462 AA.
AC   F7T063;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Biotin carboxylase {ECO:0000256|ARBA:ARBA00017242, 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|ARBA:ARBA00033786, ECO:0000256|RuleBase:RU365063};
GN   ORFNames=AXXA_11615 {ECO:0000313|EMBL:EGP46152.1};
OS   Achromobacter insuavis AXX-A.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=1003200 {ECO:0000313|EMBL:EGP46152.1, ECO:0000313|Proteomes:UP000004853};
RN   [1] {ECO:0000313|EMBL:EGP46152.1, ECO:0000313|Proteomes:UP000004853}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AXX-A {ECO:0000313|EMBL:EGP46152.1,
RC   ECO:0000313|Proteomes:UP000004853};
RA   Bador J., Amoureux L., Neuwirth C.;
RL   Submitted (JUN-2011) 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|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|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:EGP46152.1}.
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DR   EMBL; AFRQ01000042; EGP46152.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7T063; -.
DR   PATRIC; fig|1003200.3.peg.2297; -.
DR   eggNOG; COG0439; Bacteria.
DR   HOGENOM; CLU_000395_3_2_4; -.
DR   OrthoDB; 9803706at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000004853; 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; 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}; 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}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT   DOMAIN          11..456
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          130..327
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   462 AA;  50085 MW;  FDC26D736C89EE4F CRC64;
     MGMHSFYRPR RIQTLLVANR GEIALRVIRA ARELGMRTVA VYSDADRDAL AVRLADAAVH
     IGPAHATRSY LNAEALLAAA RESGADAIHP GYGFLAENAD FSQAVTDAGL VFVGPDARTI
     RSMGDKAAAR ACAKAAGVPT VPGSEGVVGS LDEALSHAAQ IGYPLMIKAS AGGGGRGIRV
     AIDEARLREA IPMAQAEARA AFGDGGVYLE RYLPRARHIE VQVLGDGERA VHLFERECSL
     QRRRQKVFEE APSPALSPAL RQALCESALR LTESVGYRGA GTLEYLYDET RGEFYFIEMN
     TRIQVEHPIT EAITGIDLVR EMLRIADGEP LRFTQSDIVM RGAAIECRLN AEDPSRNFAP
     GPGTVSHVRW PAGPGVRIDS MVYAGSVVPP YYDSLLAKLI VWDEDRDAAL ARMARALDET
     EFEGVPSTLA LHRALVADAG VMAGDYHTNY LESWMQQREG TQ
//
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