ID A0A0C2AYJ3_9ACTN Unreviewed; 774 AA.
AC A0A0C2AYJ3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Molybdopterin oxidoreductase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=QR77_08315 {ECO:0000313|EMBL:KIF73995.1};
OS Streptomyces sp. 150FB.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF73995.1, ECO:0000313|Proteomes:UP000031584};
RN [1] {ECO:0000313|EMBL:KIF73995.1, ECO:0000313|Proteomes:UP000031584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=150FB {ECO:0000313|EMBL:KIF73995.1,
RC ECO:0000313|Proteomes:UP000031584};
RA Tarkka M.T., Feldhahn L., Kruger D., Buscot F., Wubet T.;
RT "Genome sequence of the mycoparasite antagonist Streptomyces sp. strain FB
RT 150.";
RL Submitted (NOV-2014) 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:KIF73995.1}.
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DR EMBL; JTHL01000001; KIF73995.1; -; Genomic_DNA.
DR RefSeq; WP_040020653.1; NZ_JTHL01000001.1.
DR AlphaFoldDB; A0A0C2AYJ3; -.
DR STRING; 1576605.QR77_08315; -.
DR OrthoDB; 5287431at2; -.
DR Proteomes; UP000031584; 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:UP000031584}.
FT DOMAIN 120..486
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..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 774 AA; 84584 MW; 440518B7CBAEB831 CRC64;
MASKPPAGDP AQDAPRVTAP KHAAAGIPAI AHSLLISHQQ MGVRRTARTL LKLNQKKGFD
CPGCAWPEGD HRHTAEFCEN GAKAVAEEAT LRRVTPDFFE EHPVSDLFGR SGYWLGQQGR
ITHPMYLPEG ADRYEPISWD SAFEIIAEEL QALESPDEAC FYTSGRTSNE AAFLLQLFAR
EFGTNNLPDC SNMCHESSGS ALSETIGIGK GSVSLEDMHK ADLIIVAGQN PGTNHPRMLS
ALEKAKAGGA KIISVNPLPE AGLERFKNPQ TPLGMVKGAA LTDLFLQIRI GGDQALFRLL
NRLVLETPGA VDDAFIEEHT HGYEDFKAAA LAADWDETLL ATGLERAEIE KAAEMALASE
RTIVCWAMGL TQHKHSVPTI REVVNFLLLR GNIGRPGAGV CPVRGHSNVQ GDRTMGIFER
PAPAFLDALD REFSITSPRH HGYDVVRTIE AMRDGDAKVF FAMGGNFVAA TPDTEVTEAA
MRRTRLTVHV STKLNRSHVV TGVRALILPT LGRTDKDIQA GVKQIVTVED SMGMVHASRG
NLTPASPDLL SEPAIITNMA RAVLGPSSMT PWEDFEKDYA NIRDRIARVV PGFENFNERV
KRPGGFELPH GPRDTRSFPT ATGKANFTAA PVEYPRLPEG RLLLQTMRSH DQYNTTIYGL
DDRYRGIKDG RRIVMVNPDD ARELGLPDGA YTDLVSEWKD GVERRAPGFR IVHYPTARGC
AAAYYPETNV LVPLDATADT SNTPTSKSVV VRFEHTGRRE VAQSTDGDTD TDTV
//
