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
//