ID   A0A2W2DT71_9ACTN        Unreviewed;       874 AA.
AC   A0A2W2DT71;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:PZG02938.1};
GN   ORFNames=C1I99_00290 {ECO:0000313|EMBL:PZG02938.1};
OS   Micromonospora deserti.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=2070366 {ECO:0000313|EMBL:PZG02938.1, ECO:0000313|Proteomes:UP000248749};
RN   [1] {ECO:0000313|EMBL:PZG02938.1, ECO:0000313|Proteomes:UP000248749}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13K206 {ECO:0000313|EMBL:PZG02938.1,
RC   ECO:0000313|Proteomes:UP000248749};
RA   Sahin N., Saygin H., Ay H.;
RT   "Draft genome sequence of Salinispora sp. 13K206.";
RL   Submitted (JAN-2018) 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:PZG02938.1}.
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DR   EMBL; POUB01000002; PZG02938.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2W2DT71; -.
DR   OrthoDB; 9759518at2; -.
DR   Proteomes; UP000248749; 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   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:UP000248749}.
FT   DOMAIN          3..392
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          422..464
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          709..821
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   REGION          661..703
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..691
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   874 AA;  97456 MW;  C3D5CAA3C3CF6B2C CRC64;
     MVNSDCVIIQ GSNMAEAHPV GFQWAMEAKA RGAKIFHVDP RFTRTSALAS AHVPIRAGTD
     IAFLGGIVNY ILRNELDFRE YVIAYTNAAT IVSEDFRDTE ELDGLFSGYD AEKTSYDQQS
     WQYQGQEEAG RRDTVTERET AAGLGYESHG PPISGQARRD ETLQHPRCVY QILKRHYARY
     TPEMVERVCG IAREKFEEVA RAWTENSGRD RTTMLVYSVG WTQHTVGVQY IRTGAIIQLL
     LGNVGRPGGG VLALRGHASI QGSTDIPTLF DLLPGYLPKP HHASHPTFDE WVDSIRRPGQ
     KGFWGNARSY AVNLLKAYWG DAATPENDFC YGYLPRMTGD HGHYQTVFDM IDGKVKGYFL
     VGQNPAVGSA HGRAQRRGLA NLDWLVVRDL FMIESATFWK DGPEVETGEL APDRCRTEVF
     FLPAASHVEK EGTFTQTQRL VQWREKAVEP PGDCRSELWF FYHLGRIIRQ KLAASPSPRD
     QAVLDLTWDY PTSGPHDEPC AEAVLREING YEVATGRPLS SFTEMTADGA TAGGCWIYCG
     VFADGVNQAA RRKPGREQSW VAPEWGWAWP ANRRLLYNRA SADPQGRPWS ERKRYVWWDE
     ESGEWTGHDV PDFEKTKPPS YRPPDGATGV AALAGDDPFI MQGDGKGWLF APTGVLDGPL
     PTHYEPAESP VRNPLYDQQA SPARKTYQRP DNPINPSPPG PHSQVFPYVF TTARLTEHHT
     AGGMSRTVRY LAELQPEMFV EVSPELAVQL GLTHLGWAHV VTARAVIEAR VLVTDRLSPL
     RVEGRVIHQV WLPYHYGGTG LVRGESVNDL FGAVLDPHVL IQESKVGTCD IRPGRRPTGP
     ALLDFLADYR RRAGITDGPY PPIVTTDGST NREA
//