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Database: UniProt
Entry: A0A3R8VWU2_9CORY
LinkDB: A0A3R8VWU2_9CORY
Original site: A0A3R8VWU2_9CORY 
ID   A0A3R8VWU2_9CORY        Unreviewed;       593 AA.
AC   A0A3R8VWU2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   28-JUN-2023, entry version 16.
DE   RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE            EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN   ORFNames=CXF42_07235 {ECO:0000313|EMBL:RRQ03458.1};
OS   Corynebacterium bovis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=36808 {ECO:0000313|EMBL:RRQ03458.1, ECO:0000313|Proteomes:UP000278422};
RN   [1] {ECO:0000313|EMBL:RRQ03458.1, ECO:0000313|Proteomes:UP000278422}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16-2004 {ECO:0000313|EMBL:RRQ03458.1,
RC   ECO:0000313|Proteomes:UP000278422};
RA   Gulvik C.A.;
RT   "Twenty Corynebacterium bovis Genomes.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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:ARBA00024172};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13502;
CC         Evidence={ECO:0000256|ARBA:ARBA00024172};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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:RRQ03458.1}.
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DR   EMBL; PQNQ01000018; RRQ03458.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R8VWU2; -.
DR   Proteomes; UP000278422; Unassembled WGS sequence.
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   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
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; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
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; PF00364; Biotin_lipoyl; 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   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 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|ARBA:ARBA00023267};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000278422}.
FT   DOMAIN          9..453
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          130..325
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          520..593
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          505..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   593 AA;  63657 MW;  8062BFDE112EE27C CRC64;
     MSQAPEIRHI TKVLVANRGE IAVRVIRAAR DEGIDSVAVY AEPDADAPFV RMADEAFALG
     GQTPAESYLD SARILDAAAK SGADAIHPGY GFLSENADFA QAVEDAGLIW IGPSPDAIRA
     LGDKVTARHI ALAAEAPMAP GTKEPVADSD EVVAFAEEHG LPVAIKAAFG GGGRGMKVAY
     TMDEVAELFD SAVRESIAAF GRGECFVERY LDRARHVECQ VLADMHGNYV VASTRDCSLQ
     RRFQKLVEEA PAPFLTPEQT ERLHESAKAI CREAGYYGAG TVEYLVGADG LISFLEVNTR
     LQVEHPVTEQ VTGWDLVREQ FRIAEGRELS RTTDPELHGH AFEFRINGED AGSGFMPQPG
     TVTAYHEPSG PGVRMDSGVE EGAVVGGQFD SMLAKLIVWG ETREQALERS RRALDEYTVE
     GLPTVIPFHR CIVTDPAFVG DGTTFGVYTR WIEEEWDNTV EPWSADDATT GTGDTVELPT
     ERMVVEVDGR RVEIAVPGEL VAGGRSLRRP RKRSGGGSRH AVSGDTVAAP MQGTVIKILV
     ADGDTVEEGD AVVVLEAMKM ENAVKAHKSG TVTALSVTTG EGVTRGQALL DIV
//
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