ID B3RBJ9_CUPTR Unreviewed; 349 AA.
AC B3RBJ9;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Formate dehydrogenase-N major subunit, anaerobic selenopeptide {ECO:0000313|EMBL:CAQ72274.1};
DE EC=1.2.1.2 {ECO:0000313|EMBL:CAQ72274.1};
GN Name=fdoG {ECO:0000313|EMBL:CAQ72274.1};
GN OrderedLocusNames=RALTA_B1682 {ECO:0000313|EMBL:CAQ72274.1};
OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=977880 {ECO:0000313|EMBL:CAQ72274.1, ECO:0000313|Proteomes:UP000001692};
RN [1] {ECO:0000313|EMBL:CAQ72274.1, ECO:0000313|Proteomes:UP000001692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC R1 {ECO:0000313|Proteomes:UP000001692};
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(2008).
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; CU633750; CAQ72274.1; -; Genomic_DNA.
DR AlphaFoldDB; B3RBJ9; -.
DR KEGG; cti:RALTA_B1682; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_951625_0_0_4; -.
DR Proteomes; UP000001692; Chromosome 2.
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; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
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:ARBA00022485};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CAQ72274.1}.
FT DOMAIN 234..337
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 349 AA; 38768 MW; F3D636245B2185A1 CRC64;
MLHMTWDADT YHDPHHPHPE EMAKEANGYA LADAFDDTGN KVLRKGQLLD SFAQLRDDGT
TSSYCWIFTG SWTEAGNQMA RRDNTDTGLG NTPGWAWSWP ANRRILYNRA SMDEMGRPWD
PRRQILHWNG QQWTGADVPD FPLTAAPGTP VGPFIMLPEG VGRLFSAGGM IDGPFPEHYE
PVESPLAKNP LHATVTHNPT ARIFQNDAQR LGNRTDFPYV ATTYSVTELF RHWTKHSHLN
AMLQPEQFVE IGEKLAADKG IGHGDTVKIT TRRGYITAKA VVTKRMRSLQ VAGQTVEQVG
IPCHWGFEGA TRKGYLANTL APGVGDANSQ TPEFKAFLVN IEKMAGARA
//
