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Database: UniProt
Entry: A0A0U3EYG9_9ACTN
LinkDB: A0A0U3EYG9_9ACTN
Original site: A0A0U3EYG9_9ACTN 
ID   A0A0U3EYG9_9ACTN        Unreviewed;       759 AA.
AC   A0A0U3EYG9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Molybdopterin oxidoreductase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AS200_32990 {ECO:0000313|EMBL:ALV36337.1};
OS   Streptomyces sp. CdTB01.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV36337.1, ECO:0000313|Proteomes:UP000068029};
RN   [1] {ECO:0000313|EMBL:ALV36337.1, ECO:0000313|Proteomes:UP000068029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CdTB01 {ECO:0000313|EMBL:ALV36337.1,
RC   ECO:0000313|Proteomes:UP000068029};
RA   Tian Y., Zhou G., Yang H., Lu X.;
RT   "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT   bacterium tolerant to cadmium.";
RL   Submitted (DEC-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}.
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DR   EMBL; CP013743; ALV36337.1; -; Genomic_DNA.
DR   RefSeq; WP_058925935.1; NZ_CP013743.1.
DR   AlphaFoldDB; A0A0U3EYG9; -.
DR   STRING; 1725411.AS200_32990; -.
DR   KEGG; scx:AS200_32990; -.
DR   OrthoDB; 5287431at2; -.
DR   Proteomes; UP000068029; Chromosome.
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; 2.40.40.20; -; 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   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068029}.
FT   DOMAIN          120..489
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          642..749
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   759 AA;  83051 MW;  7DC48A2D102E7921 CRC64;
     MATKPPKSDP VQDAPQVAEP QHAAAGLPAI GHTLRVAQRQ MGVRRTMLTL LNVNQKDGFD
     CPGCAWPEPE HRHTAEFCEN GAKAVAEEAT LRRVTPEFFA AHTVADLAGR SGYWLGQQGR
     LTHPVYLPEG GDRYEPVSWE RAFDIVAEEI AALGSPDEAV FYTSGRTSNE AAFLYQLFAR
     ELGTNNLPDC SNMCHESSGS ALSETIGIGK GSVLLEDLYK ADLIIVAGQN PGTNHPRMLT
     ALEKAKAGGA RIITVNPLPE AGLERFKNPQ TPQGVLKGAA LTDLFLQIRI GGDQALFRLL
     NKLILQTEGA VDEEFVREHT HGYEEFAAAA EAADWDETLA ATGLAREEIE RALAMVLASK
     RTIVCWAMGL TQHKHSVPTI REVVNFLLLR GNIGRPGAGV CPVRGHSNVQ GDRTMGIFER
     PAPAFLDALE KEFGFAPPRE HGFDVVEAIR ALRDGRAKVF FAMGGNFVSA SPDTEVTEAA
     MRRARLTVHV STKLNRSHVV TGARALILPT LGRTERDLQG GGEQFVTVED SMGMVHASRG
     RLEPASRHLL SEPAIVCRLA RRVLGEGSTV PWEEFEKDYA TVRDRIARVV PGFQDFNARV
     ARPGGFALPH APRDERRFPT KTGKANFTAA PVEYPELPEG RLLLQTLRSH DQYNTTIYGL
     DDRYRGIRNG RRVVLVNPED ARRLGVADGA YVDLVGEWRD GVERRAPGFR VVHYPTARGC
     AAAYYPETNV LVPLDHTADT SNTPASKSVI VRLEQSSTD
//
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