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Database: UniProt
Entry: F8ARS2_BIFLN
LinkDB: F8ARS2_BIFLN
Original site: F8ARS2_BIFLN 
ID   F8ARS2_BIFLN            Unreviewed;       654 AA.
AC   F8ARS2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE            EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN   ORFNames=BLNIAS_00201 {ECO:0000313|EMBL:AEI96703.1};
OS   Bifidobacterium longum subsp. longum KACC 91563.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1035817 {ECO:0000313|EMBL:AEI96703.1, ECO:0000313|Proteomes:UP000008938};
RN   [1] {ECO:0000313|EMBL:AEI96703.1, ECO:0000313|Proteomes:UP000008938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KACC 91563 {ECO:0000313|EMBL:AEI96703.1,
RC   ECO:0000313|Proteomes:UP000008938};
RX   PubMed=21742881; DOI=10.1128/JB.05620-11;
RA   Ham J.S., Lee T., Byun M.J., Lee K.T., Kim M.K., Han G.S., Jeong S.G.,
RA   Oh M.H., Kim D.H., Kim H.;
RT   "Complete Genome Sequence of Bifidobacterium longum subsp. longum KACC
RT   91563.";
RL   J. Bacteriol. 193:5044-5044(2011).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; CP002794; AEI96703.1; -; Genomic_DNA.
DR   RefSeq; WP_014485306.1; NC_017221.1.
DR   AlphaFoldDB; F8ARS2; -.
DR   KEGG; blk:BLNIAS_00201; -.
DR   PATRIC; fig|1035817.4.peg.125; -.
DR   HOGENOM; CLU_000395_3_1_11; -.
DR   Proteomes; UP000008938; Chromosome.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
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; 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; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          4..444
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          123..318
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          535..611
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          454..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          620..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   654 AA;  70338 MW;  E529F3921E3E67D4 CRC64;
     MASIVKKLLI ANRGEIALRV VRTAKEMGIS TVAVYSEQDR NSRYVDMADE AYLLSGDTYK
     DTYLNEDLLI DILHKTGANA VHPGYGFLSE VPSFAQKVED AGAIWVGPHH TALVDLGDKI
     TARRVALRAK VPPVPGLSEP VTDVRTLLDF AHTHGYPIMM KRTDGGGGHG ITVVHDDEEL
     RRFYMNHDAL QGGDLKEYFI EKFVDKARHV ETQSGRDSHG NFTVYSTRDC SLQRRNQKLV
     EEAPAPFLSE EIISTLEEYS RRLFTTVGYV GLGTCEFMVT PNGKVYFLEV NPRLQVEHTV
     SEEVSGLDLV REQLNIAAGG ELTRAPELRG HSFELRITSE DPATNLTPGS GTLEKIQWPA
     GPGVRIDTGV EQGDTISPKF DSMMGKVIVT AQNRLDAVAR VRRVLDELVI EGVPTPIPLF
     KEIFRNDDFT AEHGHPFAVS TKWLERTYLN RTPASAASGQ PASLATAPGA AAPAAPDKSK
     SETFVIEMNN RRVKLTVPLD IVENITGSAR ARGAKRPTQP LRGAGLHNVA SSAAAANDGA
     KSGVIASPMQ AVVTRINVSE GQQVAKGDLL VVLESMKMEN YVYAPAAGEV KKIFVGPADG
     VEAGDTLVTL DVNAGKAKAA AAAPGSLPQA AASTAPSSEG ADKATDAKKE GGND
//
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