ID   A0A0A8ETE1_9ACTN        Unreviewed;       761 AA.
AC   A0A0A8ETE1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:AJC59103.1};
GN   ORFNames=GZL_06534 {ECO:0000313|EMBL:AJC59103.1};
OS   Streptomyces sp. 769.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1262452 {ECO:0000313|EMBL:AJC59103.1, ECO:0000313|Proteomes:UP000031113};
RN   [1] {ECO:0000313|EMBL:AJC59103.1, ECO:0000313|Proteomes:UP000031113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=769 {ECO:0000313|EMBL:AJC59103.1,
RC   ECO:0000313|Proteomes:UP000031113};
RA   Du Q., Wang Q., Li Q., Wang L., Zhang Z., Ren J., Wang J., Wang M.;
RT   "Complete Genome Sequence of Streptomyces gongzhulingensis.";
RL   Submitted (DEC-2012) 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; CP003987; AJC59103.1; -; Genomic_DNA.
DR   RefSeq; WP_039637502.1; NZ_CP003987.1.
DR   AlphaFoldDB; A0A0A8ETE1; -.
DR   KEGG; stre:GZL_06534; -.
DR   HOGENOM; CLU_000422_16_1_11; -.
DR   Proteomes; UP000031113; 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}.
FT   DOMAIN          120..496
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          644..750
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   761 AA;  82670 MW;  503A3D56859EC9B5 CRC64;
     MAGKPPASDP VQDAPEVGAP QHSAVGIPAI THALKISQQQ MGVRRTALTL LRVNQKNGFD
     CPGCAWPEDD KRHAAEFCEN GAKAVAEEAT LRRVTPDFFA AHSVADLASR SGYWLGQQGR
     LTHPMYLPEG ADHYEPVTWD RAFDLIAEDL TALASPDEAV FYTSGRTSNE AAFLYQLFAR
     EFGTNNLPDC SNMCHESSGS ALTATLGVGK GSVLLEDLYK ADLIIVAGQN PGTNHPRMLS
     ALEKAKAGGA KIISINPLPE AGLERFKNPQ TPRGLAGGGT ALTDLFLQVR IGGDQALFRA
     LNRRILQTEG ALDEDFIRDH THGFEEFADL VRAGDDADDT LRATGLTHDE IERAAAMVLA
     SRRTIVCWAM GLTQHKHSVP TIQEVVNFLL LRGNIGRPGA GVCPVRGHSN VQGDRTMGIF
     ERPAPAFLDA LEKEFGFTPP REHGYDVVRA IRALRDGQAK VFFAMGGNFV SATPDTDVTE
     AAVRRARLTV HVSTKLNRSH AVTGARALIL PTLGRTERDR QASGDQFVTV EDSMGMVHAS
     RGRLEPAGPQ LLSEPAIVAR LAHRVLGDRS NTPWQAFEKD YATIRDRIAR VIPGFEDFNA
     KVARPGGFTL PHAPRDSRSF PTATGKANFT AAPVEHPTAP EGRLLLQTLR SHDQYNTTIY
     GLDDRYRGIK NGRRVVLVHP DDAHHLGFAD GSYADLVSEW TDGSERRAPG FRVVHYPTAR
     GCAAAYYPET NVLVPLDHTA DTSNTPASKS LVIRLEAARE G
//