ID   W9G3N9_9MICO            Unreviewed;       890 AA.
AC   W9G3N9;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:EWT00615.1};
GN   ORFNames=N865_14335 {ECO:0000313|EMBL:EWT00615.1};
OS   Intrasporangium oryzae NRRL B-24470.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=1386089 {ECO:0000313|EMBL:EWT00615.1, ECO:0000313|Proteomes:UP000019489};
RN   [1] {ECO:0000313|EMBL:EWT00615.1, ECO:0000313|Proteomes:UP000019489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-24470 {ECO:0000313|EMBL:EWT00615.1,
RC   ECO:0000313|Proteomes:UP000019489};
RA   Liu H., Wang G.;
RT   "Intrasporangium oryzae NRRL B-24470.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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:EWT00615.1}.
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DR   EMBL; AWSA01000038; EWT00615.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9G3N9; -.
DR   STRING; 1386089.N865_14335; -.
DR   PATRIC; fig|1386089.3.peg.3146; -.
DR   eggNOG; COG0243; Bacteria.
DR   OrthoDB; 9759518at2; -.
DR   Proteomes; UP000019489; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR048158; Formate_DH_Act.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   NCBIfam; NF041513; formate_DH_Act; 1.
DR   PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR   PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR   Pfam; PF00384; Molybdopterin; 2.
DR   Pfam; PF01568; Molydop_binding; 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:ARBA00022485};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019489}.
FT   DOMAIN          2..406
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          436..479
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          724..843
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   REGION          125..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   890 AA;  98076 MW;  FD78F88A957EBFB4 CRC64;
     MSNADCIVIQ GSNMAECHPV AYQWVMEARL KGARVIHIDP RFTRTSATAD KHIPIRAGSD
     VVLLGALINH IISNELYFKE YVVAYTNAAT LVSPEFQDTE DLDGLFSGYD DEKGSYKQDT
     WAYASADGEG DESPGTIGGP AAVHEHGQTE SERSAGEQHG SGGPALEHAR VLRDETLQDP
     NTVFQILKRH YSRYTPEMVA DACGISVDDF HYLAEAVTEN SGRERTTAFV YAVGWTQHTL
     GAQFIRTAAI VQLLLGNMGR PGGGIMALRG HASIQGSTDI PTLYNLLPGY LAMPVAGLHD
     TWEAYLGAIA NKEQKGFWAN ADTYAVSLLK AWWGKAATAE NNWRFDYLPR LSGAHGTYQT
     TMAMLDGEVE GYFLLGQNPA VGSAHGRMQR RAMSHLKWLV VRDFNMIESA TFWKDGPEIV
     SGELVTEDIE TEVFFLPAAA HTEKSGSFTQ TQRMLQWHHQ AVQPPGDCQS ELQFFYELGR
     RVRELLADST DERDRPLLDL TWDYPTDGHG EPDAEAVLAE INGRHLTGDK AGQPLSSYTE
     MKADGSTEGG CWIYTGVYAD GVNHAANRKP GREQDLTALE WGWAWPANRR ILYNRASADP
     DGKPWSERKK YVWWDEEQGR WTGHDVPDFV PDKAPTYRPE PGTGGPAGLA GDDPFVMQAD
     GKGWLFTPKG MLDGPLPTHY EPQESPVRNP LYGQQSNPAR KVFPRKDNLW SPSGGERGSE
     VYPFVFTTYR LTEHHTAGGM SRWLPYLAEL QPEFFCEVSP ELAAERGLEN GGWATIVSAR
     TAIEARVLVT ERMTPLVVGG HTIHQVGLPY HWGVGKEALV SGDAANDLLG VALDPNVQIQ
     ESKAGSCDIV AGRRPQGEAL LRLVEEYQSR AGSTVMTGNV LVTPPEEESR
//