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Database: UniProt
Entry: A0A4R1DQ57_9ACTN
LinkDB: A0A4R1DQ57_9ACTN
Original site: A0A4R1DQ57_9ACTN 
ID   A0A4R1DQ57_9ACTN        Unreviewed;       759 AA.
AC   A0A4R1DQ57;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=FdhF/YdeP family oxidoreductase {ECO:0000313|EMBL:TCJ45078.1};
GN   ORFNames=E0500_19815 {ECO:0000313|EMBL:TCJ45078.1};
OS   Streptomyces sp. KM273126.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2545247 {ECO:0000313|EMBL:TCJ45078.1, ECO:0000313|Proteomes:UP000294981};
RN   [1] {ECO:0000313|EMBL:TCJ45078.1, ECO:0000313|Proteomes:UP000294981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KM273126 {ECO:0000313|EMBL:TCJ45078.1,
RC   ECO:0000313|Proteomes:UP000294981};
RA   Ng Z.Y., Tan G.Y.A.;
RT   "Novel actinobacteria from marine sediment.";
RL   Submitted (MAR-2019) 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:TCJ45078.1}.
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DR   EMBL; SJXB01000080; TCJ45078.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R1DQ57; -.
DR   OrthoDB; 5287431at2; -.
DR   Proteomes; UP000294981; 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:UP000294981}.
FT   DOMAIN          120..491
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;  83054 MW;  C370CCE2FBDE430D CRC64;
     MATKPPKGDP VQDAPQVAGP KHAAAGLPAV GHSLRIAQQQ MGVKRTALTL LRVNQKDGFD
     CPGCAWPEPE HRHTAEFCEN GAKAVAEEAT LRRVTPEFFA AHTVADLATR SGYWLGQQGR
     LTHPMYLPEG GEHYEPVSWD RAFDIVAEEL KALQSPDEAL FYTSGRTSNE AAFLYQLFAR
     EFGTNNLPDC SNMCHESSGS ALSETLGVGK GSVLLDDLYK ADLIIVAGQN PGTNHPRMLS
     ALEKAKANGA RIITVNPLPE AGMERFKNPQ TPQGMLKGAA LTDLFLQIRI GGDQALFRLL
     NKLILATDGA VDEDFVREHT HGYEEFAEAA RAADWDETLT ATGLTQEEIN EALGMVLASQ
     RTIVCWAMGL TQHKHSVPTI REVVNFLLLR GNIGRPGAGV CPVRGHSNVQ GDRTMGIFER
     PAPAFLDALE KEFGFAPPRE HGYDVVRAIR AMRDDKAKVF FAMGGNFVSA SPDTEVTEAA
     MRRAHLTVHV STKLNRSHAV TGARALVLPT LGRTERDLQG SGEQFVTVED SMGMVHASRG
     RLEPASDHLL SETAIVCRLA RRVLGEDSRT PWEEFEKDYA TIRDRIARVV PGFDDFNARV
     ARPEGFALPH APRDERRFPT GTGKANFTAA PVEYPELPAG RLLLQTLRSH DQYNTTIYGL
     DDRYRGIRNG RRVVLVNPED AAELQVADGS YVDLVGEWKD GVERRAPGFR VVHYPTARGC
     AAAYYPETNV LVPLDATADT SNTPASKSVV VRLEQSGTD
//
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