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Database: UniProt
Entry: A0A0M9YB25_9ACTN
LinkDB: A0A0M9YB25_9ACTN
Original site: A0A0M9YB25_9ACTN 
ID   A0A0M9YB25_9ACTN        Unreviewed;       756 AA.
AC   A0A0M9YB25;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Molybdopterin oxidoreductase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ADK55_34940 {ECO:0000313|EMBL:KOU38300.1};
OS   Streptomyces sp. WM4235.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415551 {ECO:0000313|EMBL:KOU38300.1, ECO:0000313|Proteomes:UP000037699};
RN   [1] {ECO:0000313|EMBL:KOU38300.1, ECO:0000313|Proteomes:UP000037699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM4235 {ECO:0000313|EMBL:KOU38300.1,
RC   ECO:0000313|Proteomes:UP000037699};
RA   Noorani M.;
RL   Submitted (JUL-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:KOU38300.1}.
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DR   EMBL; LGDE01000470; KOU38300.1; -; Genomic_DNA.
DR   RefSeq; WP_053684907.1; NZ_LGDE01000470.1.
DR   AlphaFoldDB; A0A0M9YB25; -.
DR   PATRIC; fig|1415551.3.peg.7619; -.
DR   OrthoDB; 5287431at2; -.
DR   Proteomes; UP000037699; 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   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:UP000037699}.
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..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   756 AA;  81999 MW;  233792749E7F24C9 CRC64;
     MATKPPAGDP VQDSPRIAPP GRAAAGLPAI GHTLRIAQQQ MGLARTARTL LKVNQKDGFD
     CPGCAWPEGD KRHTAEFCEN GAKAVAEEAT LRRVTPEFFA AHPLADLEGR SGYWLGQQGR
     ITEPMLLPEG GDRYEPVSWE RAFAIIAEEL TALGSPDEAL FYTSGRTSNE AAFLFQLFAR
     EFGTNNLPDC SNMCHESSGS ALNETIGIGK GSVSLEDLHQ AELIIVAGQN PGTNHPRMLS
     ALERAKSAGA KIISVNPLPE AGMERFKNPQ TPLGMLRGTA LNDLFLQIRI GGDQALFRLL
     NKLVIETDGA TDEEFIREHT HGYEDLAAAA AKTDWDETLT ATGLTRPEIE SALAMVLASK
     RTIVCWAMGL TQHKHSVATI REVVNLLLLR GDIGRPGAGV CPVRGHSNVQ GDRTMGIFER
     PAPAFLDALD REFGITSPRR HGFDVVRSIE ALRDGEAKVL FAMGGNFVGA TPDTAVTEAA
     IRRASLTVHV STKLNRSHAV TGRRALILPT LGRTDKDVQA AGRQFVTVED SMGMVHASRG
     NLAPASPHLL SEPAIVARLA RAVLGAASAT PWEEFERDYG TIRDRISRVV PGFEDFNARA
     ARPEGFRLPH APRDERRFPT KTGKANFTAA PVEYPRVPEG RLLLQTLRSH DQYNTTIYGL
     DDRYRGITGG RRVVMVNPLD AAELGLVDGA YTDIVGEWRD GVERRAPGFR IVHYPTARGC
     AAAYYPETNV LVPLDSTADT SNTPASKSVV VRFEPA
//
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