ID A0A261F2Y3_9BIFI Unreviewed; 632 AA.
AC A0A261F2Y3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=PSSU_0217 {ECO:0000313|EMBL:OZG53451.1};
OS Pseudoscardovia suis.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Pseudoscardovia.
OX NCBI_TaxID=987063 {ECO:0000313|EMBL:OZG53451.1, ECO:0000313|Proteomes:UP000216454};
RN [1] {ECO:0000313|EMBL:OZG53451.1, ECO:0000313|Proteomes:UP000216454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24744 {ECO:0000313|EMBL:OZG53451.1,
RC ECO:0000313|Proteomes:UP000216454};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
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:OZG53451.1}.
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DR EMBL; MWWQ01000004; OZG53451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261F2Y3; -.
DR Proteomes; UP000216454; 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; 3.30.470.20; 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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OZG53451.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000216454}.
FT DOMAIN 8..448
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 127..322
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 526..609
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 517..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 632 AA; 68164 MW; A3462AC6BBDCAA8F CRC64;
MTDSQLTHIS KLLVANRGEI ALRVIRTARE MGIATVAVYS ESDRDAPFAS AADEAYRLPG
DTYAETYLNE SLIIDVARRS GADAIHPGYG FLSEVPSFAK AVLDAGLIWV GPKPDVLVDL
GDKITARRFA ERADVSPVPG ISEPVTDIAT LLRFCHDYGY PVMLKRTDGG GGHGITVVRD
DDALRSFFMS HDALQGGDLG KYFIEKFVAK SRHVETQCGR DSHGNFTVYS TRDCSVQRRN
QKLIEEAPAP FLTAKENARL VTYSRRLFEA ANYVGLGTCE FMLTPTQDIY FLEVNPRLQV
EHTVSEEVCG IDLVREQLVI ADGGTLTQAG EPRGHSFELR ITSENPDTNL APGSGTIETL
EFPSGPGVRV DFGVKQGSVI SPKFDSMMGK IIVTAQNRQA AIARVLRALG EFKLEGVSTP
CSLFATIFQD PDFIGDDHGF AVTTKWLEGK YLTKKPASAK AGQPASLTAG LDTAPTQAEQ
PRESFVFEVN DKRVQVTIPE EFIGALGARG AHAGRRRAQP LRGAGTQVTG APQQRGGLHD
GNICSPMQAV VTRVNAAADE HVNKGDLLIV LESMKMENYV YAPAAGTVKE ILVGPSDGVD
AGEPLVSFDV DSAKGSDKTA TKNANNTAAK EE
//
