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Database: UniProt
Entry: A0A0N0SHN0_9ACTN
LinkDB: A0A0N0SHN0_9ACTN
Original site: A0A0N0SHN0_9ACTN 
ID   A0A0N0SHN0_9ACTN        Unreviewed;       546 AA.
AC   A0A0N0SHN0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE            EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN   ORFNames=ADK56_15490 {ECO:0000313|EMBL:KOU50218.1};
OS   Streptomyces sp. MMG1522.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415545 {ECO:0000313|EMBL:KOU50218.1, ECO:0000313|Proteomes:UP000037713};
RN   [1] {ECO:0000313|EMBL:KOU50218.1, ECO:0000313|Proteomes:UP000037713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMG1522 {ECO:0000313|EMBL:KOU50218.1,
RC   ECO:0000313|Proteomes:UP000037713};
RA   Noorani M.;
RL   Submitted (JUL-2015) 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:KOU50218.1}.
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DR   EMBL; LGDF01000115; KOU50218.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0SHN0; -.
DR   PATRIC; fig|1415545.3.peg.3331; -.
DR   Proteomes; UP000037713; 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}.
FT   DOMAIN          1..405
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          81..278
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          467..545
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          460..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   546 AA;  57274 MW;  4191DEF6D980F501 CRC64;
     MHVRAADEAF ALGGDTPAAS YLDMAKVLQA AADSGADAIH PGYGFLSENA EFAQAVLDAG
     LTWIGPPPQA IRDLGDKVAA RHIAQRAGAP LVAGTPDPVS GSDEVVAFAE EHGLPIAIKA
     AFGGGGRGLK VARTLEEIPE LYDSAVREAV AAFGRGECFV ERYLDKPRHV ETQCLVDSHG
     NVVVVSTRDC SLQRRHQKLV EEAPAPFLSQ AQNDELYAAS KAILKEAGYV GAGTVEFLVG
     LDGTISFLEV NTRLQVEHPV TEEVTGIDLV REMFRIADGE ELGYGDPAVR GHSFEFRING
     EDPGRGFLPA PGTVTLFAPP TGPGVRLDAG VESGSVIGPA WDSLLAKLVI TGATREQALQ
     RAARALAEFQ VEGMATAIPF HRAVVVDPAF TADPFTVHTR WIETEFVNEI KPFAAPADAD
     AEDEAGRETV VVEVGGKRLE VSLPSSLGMS LARTGLAAGA KPKRRAAKKA GSAASGDSLA
     SPMQGTIVKI AVEEGQEVKE GDLVVVLEAM KMEQPLNAHR SGTIKGLSAA VGASVSSGAL
     ICEIKD
//
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