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
//