ID   A0A1G4XGB0_9ACTN        Unreviewed;       901 AA.
AC   A0A1G4XGB0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Formate dehydrogenase major subunit {ECO:0000313|EMBL:SCX40196.1};
GN   ORFNames=SAMN03159343_0906 {ECO:0000313|EMBL:SCX40196.1};
OS   Klenkia marina.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Klenkia.
OX   NCBI_TaxID=1960309 {ECO:0000313|EMBL:SCX40196.1, ECO:0000313|Proteomes:UP000198981};
RN   [1] {ECO:0000313|Proteomes:UP000198981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45722 {ECO:0000313|Proteomes:UP000198981};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FMUH01000001; SCX40196.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4XGB0; -.
DR   STRING; 1960309.SAMN03159343_0906; -.
DR   OrthoDB; 9759518at2; -.
DR   Proteomes; UP000198981; 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}.
FT   DOMAIN          18..402
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          432..474
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          714..831
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   REGION          145..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          617..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          860..901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        877..901
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   901 AA;  99171 MW;  D264BDF0FCF1D598 CRC64;
     MPGLGATYGR GGATGFQQDL VNADCIVIEG SNMAECHPVG FQWVMEAKAR GAKVIHIDPR
     FTRTSAVSDT HVPLRAGTDI AFLGGLISYV LENELDFRDY VLAYTNASSL VGEDFVDTED
     LDGLFSGWDQ DSKSYDKTSW QFEGAHEPSA TGTDEIDPPA PQKDSLGQPV TDPTLQHPRS
     VYQVMKRHFA RYTPEMVGDI CGIEPEVFLD VARAVTANSG RDRTTAWVYS VGWTHHTVGV
     QYIRTAGILQ ALLGNMGRPG GGILALRGHA SIQGSTDIPT LYNLLPGYLP MPHAEEHATL
     DDFCKVGDEM VGFWGGTRAY MVSLLKAWFG DAATAENDWC YDLLPKINGD HGSYRQVADM
     IQGKIPGYFL VGENPAVGHA NGKMQRLGLA NLDWLVVRDL QMIESATFWQ TAPEIATGEL
     VTDQIGTEVF FMPAATHTEK EGTFTNTQRV LQWHRQAIEP PDDARSDLWF YFHLGRILRD
     RLRDSTDPRD RGLQALTWDY PTHGPLVEPS AEAVLREING VGPDGKALSS YTELKDDGTT
     TAGCWIYTGV YADEVNQSDR RKPGREQNWV APEWGWAWPA NRRTLYNRAS ADPEGKPWSE
     RKAYVWWDED AQRWTGHDVP DFEATKPPSY RPEPGAKGAA GISGADAFIM QNDGKAWLYA
     PSGLADGPLP THYEPDESPM PNLLYRQQAN PGREVIEAAW NRSNPPTSDV YPYAFTTYRL
     TEHHTAGGMS RTLPYLAELQ PEFFVEVSPQ LAHERGLENG GWATLVSART AIEARVLVTE
     RMRPLKVGGG RVVHQIGVPY HWGEQGISTG DSGNDLFGVV MDPNVHIQES KVATCDIQAG
     RRPRGPALVD LVESYRQRAG VKSGRVPVGG RSPVEETNMT GEDSGADTTQ SAPDHIAEGT
     S
//