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Database: UniProt
Entry: A0A1B6ALB5_9ACTN
LinkDB: A0A1B6ALB5_9ACTN
Original site: A0A1B6ALB5_9ACTN 
ID   A0A1B6ALB5_9ACTN        Unreviewed;       777 AA.
AC   A0A1B6ALB5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:GAU68351.1};
GN   ORFNames=SSP35_07_01530 {ECO:0000313|EMBL:GAU68351.1};
OS   Streptomyces sp. NBRC 110611.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1621259 {ECO:0000313|EMBL:GAU68351.1, ECO:0000313|Proteomes:UP000094479};
RN   [1] {ECO:0000313|EMBL:GAU68351.1, ECO:0000313|Proteomes:UP000094479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 110611 {ECO:0000313|EMBL:GAU68351.1,
RC   ECO:0000313|Proteomes:UP000094479};
RA   Igarashi Y., Komaki H., Ichikawa N., Hosoyama A., Fujita N., Panbangred W.;
RT   "Whole genome shotgun sequence of Streptomyces sp. NBRC 110611.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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:GAU68351.1}.
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DR   EMBL; BBUY01000007; GAU68351.1; -; Genomic_DNA.
DR   RefSeq; WP_066932393.1; NZ_BBUY01000007.1.
DR   AlphaFoldDB; A0A1B6ALB5; -.
DR   STRING; 1621259.GCA_001590865_03667; -.
DR   OrthoDB; 5287431at2; -.
DR   Proteomes; UP000094479; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   CDD; cd02787; MopB_CT_ydeP; 1.
DR   CDD; cd02767; MopB_ydeP; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR037951; MopB_CT_YdeP.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR010046; Mopterin_OxRdtse_a_bac.
DR   InterPro; IPR041953; YdeP_MopB.
DR   NCBIfam; TIGR01701; Fdhalpha-like; 1.
DR   PANTHER; PTHR43105:SF4; PROTEIN YDEP; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   PIRSF; PIRSF000144; CbbBc; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094479}.
FT   DOMAIN          120..511
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          660..767
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   REGION          331..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..354
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   777 AA;  84102 MW;  145595ADD7357022 CRC64;
     MAGKPPSSDP IQDAPQVGEP QHAAVGLPAI THALRISQKQ MGVRRTALTL LRVNQQNGFD
     CPGCAWPEPD KPHTAEFCEN GAKAVAEEAT LRRVTPDFFA AHSVADLATR SGYWLGQQGR
     LTHPMYLPEG ADHYVPVPWE QAFDIIGEEL TALDSPDEAV FYTSGRTSNE AAFLYQLFAR
     EFGTNNLPDC SNMCHESSGS ALTETLGVGK GSVLLEDLYQ ADLIIVAGQN PGTNHPRMLT
     ALEKAKAGGA KIISINPLPE AGLERFKNPQ TPRGLAGGGT ALTDLFLQVR LGGDQALFRA
     FNRRILDTPG AVDEDFIREH THGFEEFARL ARGGGDNADN GGSESGSDSS GIDDETLAAT
     GLTHEEIDRA LEMILASRRT IVCWAMGLTQ HKHAVPTIQE VVNFLLLRGN IGRPGAGVCP
     VRGHSNVQGD RTMGIFERPA PAFLDALEKE FGFAPPREHG LDVVRAIHAL RDGRAKVFLA
     MGGNFVAATP DTDVTEAAMR RARLTVHIST KLNRSHAVTG THALILPTLG RTERDLQASG
     EQFVTVEDSM GMVHASRGRL EPAGPHLLSE TAIVTRLARR VLGPGSHTPW EQFEQDYAAI
     RDRIAHVIPG FENFNTKVAH PGGFALPHAP RDSRHFPTAT GKANFTAAPV TYPAVPEGRL
     LLQTLRSHDQ YNTTIYGLDD RYRGIKNGRR VVLVHPDDAR ERGLADGAYT DLVSEWTDGS
     ERRATGFRVV HYPTARGCAA AYYPETNVLI PLDHTADTSN TPAAKSVVIR LESAAQG
//
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