ID   F2RGV8_STRVP            Unreviewed;       760 AA.
AC   F2RGV8;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Putative formate dehydrogenase oxidoreductase protein {ECO:0000313|EMBL:CCA54919.1};
GN   OrderedLocusNames=SVEN_1632 {ECO:0000313|EMBL:CCA54919.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS   4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA54919.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA54919.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA54919.1};
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in actinomycetes.";
RL   BMC Genomics 12:175-175(2011).
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; FR845719; CCA54919.1; -; Genomic_DNA.
DR   RefSeq; WP_015032837.1; NZ_JABVZO010000078.1.
DR   AlphaFoldDB; F2RGV8; -.
DR   STRING; 953739.SVEN_1632; -.
DR   GeneID; 69863808; -.
DR   KEGG; sve:SVEN_1632; -.
DR   PATRIC; fig|953739.5.peg.3742; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_16_1_11; -.
DR   OrthoDB; 5287431at2; -.
DR   Proteomes; UP000006854; 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; 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:UP000006854}.
FT   DOMAIN          120..488
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          643..750
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   760 AA;  82482 MW;  2587F52027433FB4 CRC64;
     MVSKPPVGDP VQDAPQVTPP QHAAAGLPAI GHTLRIAQEQ MGLRRTARTL LKVNQKDGFD
     CPGCAWPEAD KRHVAEFCEN GAKAVAEEAT LRRVTPEFFA AHPVADLATR SGYWLGQQGR
     ITQPMLLAED GDRYEPVSWE RAFAIIAEEL RALASPDEAL FYTSGRTSNE AAFLLQLFAR
     EFGTNNLPDC SNMCHESSGS ALTETIGIGK GSVSLEDLHR ADLIIVAGQN PGTNHPRMLS
     ALEKAKAGGA RIISVNPLPE AGLERFKNPQ TPQGMLRGAA LGDLFLQIRI GGDQALFRLL
     NKLVLETPGA VDEEFVRDHT HGYEEFVTAA KEADWDETLA ATGLGRAEIE RALEMVLASE
     RTVVCWAMGL TQHKHSVPTI REVVNFLLLR GNIGRPGAGV CPVRGHSNVQ GDRTMGIFER
     PAPAFLDALD KEFGIVSPRH HGFDVVRSIQ ALRDGEAKVF FAMGGNFVGA TPDTEVTEAA
     MRRARLTVHV STKLNRSHAV TGTRALILPT LGRTDKDVQA SGKQFVTVED SMSLVHASRG
     NLPPASPHLL SEPAIVARMA RAVLGDGSAT PWEEFEADYA AIRDRIARVV PGFQDFNARL
     AADPGGFRLP HGPRDERRFP TATGKANFTA APVEYPKVPE GRLLLQTLRS HDQYNTTIYG
     LDDRYRGIKG GRRVVLVHPR DAAAAGFEDG AYVDLVSEWT DGSERRAPGF RLVHYPTSRG
     CAAAYYPETN VLVPLESTAD VSNTPASKSV IVRLEQSPSA
//