ID   W5TP35_9NOCA            Unreviewed;       766 AA.
AC   W5TP35;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Putative formate dehydrogenase {ECO:0000313|EMBL:AHH20718.1};
GN   ORFNames=NONO_c59410 {ECO:0000313|EMBL:AHH20718.1};
OS   Nocardia nova SH22a.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH20718.1, ECO:0000313|Proteomes:UP000019150};
RN   [1] {ECO:0000313|EMBL:AHH20718.1, ECO:0000313|Proteomes:UP000019150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH22a {ECO:0000313|EMBL:AHH20718.1};
RX   PubMed=24747905;
RA   Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT   "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT   Analysis of the Complete Genome of Nocardia nova SH22a.";
RL   Appl. Environ. Microbiol. 80:3895-3907(2014).
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; CP006850; AHH20718.1; -; Genomic_DNA.
DR   RefSeq; WP_025352075.1; NZ_CP006850.1.
DR   AlphaFoldDB; W5TP35; -.
DR   STRING; 1415166.NONO_c59410; -.
DR   KEGG; nno:NONO_c59410; -.
DR   PATRIC; fig|1415166.3.peg.6121; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_16_1_11; -.
DR   OrthoDB; 5287431at2; -.
DR   Proteomes; UP000019150; 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:UP000019150}.
FT   DOMAIN          121..495
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          648..748
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   766 AA;  83663 MW;  4D54455AAA8D28F4 CRC64;
     MHRKPPIRDI DETDLAVTPP KEQAAGVTAV AVALERAVEE MGVVRTARTL ARVNQRHGFD
     CPGCAWPEPT GHRRPAEFCE NGAKAVAEEA TLRTVTPEFL ATHSVAELAG KSGYWLGQQG
     RITHPMVLRP GDTHYSPIEW AEAYRLIATT LRELDSPSEA LFYTSGRTAN ETAFLYQLLV
     RSFGTNNLPD CSNMCHESSG TALTKSIGIG KGSVSIDDFA AADLIIVAGQ NPGTNHPRML
     SALSNAKEHG ARVIAVNPLP ETGLIGFRDP QTVKGFTSGV TIADDFLQIR LGGDMALFQG
     LAKLLFEAED RAPGAVVDRL FVDAHTAGFA EYEKQMRAVD LGDVLTATGL TREQLDHTAE
     LLARSKATII CWAMGLTQQR HGVATIEEAT NLLLLRGMIG KPGAGVCPVR GHSNVQGDRT
     MGIWEKMPET FLAALDSEFG ISAPREHGWD TVDSIRAMRD GRAKVFIGMG GNFVSATPDT
     EVTEAALRRC ELTVQVSTKL NRSHVVHGRT ALILPTLGRT DLDVRNGVKQ QVSVEDSMSM
     VHLSTGRLQP VGDQLRSEVA IVCELAAELF GPGHPVPWAQ FRDDYDRIRD AISRVVPGCA
     DYNRKVRDRN GFQLPHPPRD SREFRTGTGK ANFAVNDLEW PRIPAGRLLL QTLRSHDQYN
     TTIYGLDDRY RGIHNARRVV LVHPDDIAEF GFADGDSVDL ISEFDDGTER RVGGFRIVGY
     STPRGNAAAY YPETNPLVPL DHVAKGSNTP VSKAVVIRLE PHHHTT
//