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Database: UniProt
Entry: R1IFE6_9PSEU
LinkDB: R1IFE6_9PSEU
Original site: R1IFE6_9PSEU 
ID   R1IFE6_9PSEU            Unreviewed;       663 AA.
AC   R1IFE6;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE            EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN   ORFNames=H480_07823 {ECO:0000313|EMBL:EOD69124.1};
OS   Amycolatopsis vancoresmycina DSM 44592.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=1292037 {ECO:0000313|EMBL:EOD69124.1, ECO:0000313|Proteomes:UP000014139};
RN   [1] {ECO:0000313|EMBL:EOD69124.1, ECO:0000313|Proteomes:UP000014139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44592 {ECO:0000313|EMBL:EOD69124.1,
RC   ECO:0000313|Proteomes:UP000014139};
RA   Kumar S., Kaur N., Kaur C., Raghava G.P.S., Mayilraj S.;
RT   "Draft genome sequence of Amycolatopsis vancoresmycina strain DSM 44592T.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:EOD69124.1}.
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DR   EMBL; AOUO01000086; EOD69124.1; -; Genomic_DNA.
DR   AlphaFoldDB; R1IFE6; -.
DR   PATRIC; fig|1292037.4.peg.1514; -.
DR   eggNOG; COG4770; Bacteria.
DR   Proteomes; UP000014139; 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; 3.30.700.40; -; 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; PS00866; CPSASE_1; 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          3..450
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          122..321
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          582..657
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   663 AA;  70080 MW;  769E5E5C85522464 CRC64;
     MMMFDSVLVA NRGEIAVRVI RTLRALGIRA VAVYSDADAD ARHVREAHTA VRIGPAEAAK
     SYLDIEAIVG AAVSSGAQAV HPGYGFLAEN AEFARACEAA GLVFIGPPVA AIDAMGDKIR
     AKATVSKAGV PVVPGASDVD IPEGGFAEAA AKVGYPLLLK PSAGGGGKGM RLVHAPEELD
     AAIESARREA KGSFGDDTLL MERFVTTPRH IEIQVLADTH GHVLHLGERE CSLQRRHQKI
     IEEAPSVLLD EATREKMGSA AAEAARSVGY VGAGTVEFIM SAKNPDEFFF MEMNTRLQVE
     HPVTELVTGL DLVEWQVRVA AGERLTLTQD DVVLNGHAVE ARVYAEDPAR GFIPTGGTVL
     AVHEPAGDGV RVDSWMTPGA VIGSNYDPML AKVIAWGPDR ASALHRLDLA LADTALLGVG
     TNTAFLRALL ADADVRAGRL DTELVDRRLA DLVSPDVPAE FFVAAALDRF LELQPAGPVV
     DPWDVPDGWR MGGSGGVTFR LKSGPARAVV RVQGTPSDAT VFVGDEAPVR VSARRDGDVL
     EIRHAGGFHR YRQACGPDRT VWLSRDGLSF PFGEQEFVLA SRGEAAGAGP VTSPMPGTVL
     VVKVAAGDVV KAGAPLLVVE AMKMEHTVTA PIDGVVSELP VRTGQQVALD ETLAVVTPQE
     EQQ
//
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