ID A0A1H3C847_9BURK Unreviewed; 196 AA.
AC A0A1H3C847;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Formate dehydrogenase (Quinone-dependent) catalytic subunit {ECO:0000313|EMBL:SDX50220.1};
GN ORFNames=SAMN04515617_104153 {ECO:0000313|EMBL:SDX50220.1};
OS Collimonas sp. OK242.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Collimonas.
OX NCBI_TaxID=1798195 {ECO:0000313|EMBL:SDX50220.1, ECO:0000313|Proteomes:UP000198586};
RN [1] {ECO:0000313|EMBL:SDX50220.1, ECO:0000313|Proteomes:UP000198586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK242 {ECO:0000313|EMBL:SDX50220.1,
RC ECO:0000313|Proteomes:UP000198586};
RA de Groot N.N.;
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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; FNOR01000004; SDX50220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3C847; -.
DR STRING; 1798195.SAMN04515617_104153; -.
DR Proteomes; UP000198586; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 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; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF10518; TAT_signal; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS51318; TAT; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..196
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011765120"
FT DOMAIN 44..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 196 AA; 21447 MW; BEA1319E3246758E CRC64;
MVHMSRRQFL KTTGATLAGS SLALMGFSPA PALAEVRSYK LTRTVETRNT CPYCSVSCGV
LMYSLGDGAK NAQASIIHIE GDPDHPVNRG TLCPKGAALL DFVHSPSRLR FPEYRAPGAK
EWKRMSWDDA LSRIATLMKQ DRDANFVEKT PEGLTVNRWL TTGMLAASAS SNEVGYLTHK
TIRSLGILGF DNQARV
//
