ID A0A1H9W7Y1_9RHOB Unreviewed; 928 AA.
AC A0A1H9W7Y1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=SAMN04490244_109173 {ECO:0000313|EMBL:SES29879.1};
OS Tranquillimonas rosea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tranquillimonas.
OX NCBI_TaxID=641238 {ECO:0000313|EMBL:SES29879.1, ECO:0000313|Proteomes:UP000198885};
RN [1] {ECO:0000313|EMBL:SES29879.1, ECO:0000313|Proteomes:UP000198885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23042 {ECO:0000313|EMBL:SES29879.1,
RC ECO:0000313|Proteomes:UP000198885};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000455};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC molybdopterin-containing oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00007023}.
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DR EMBL; FOGU01000009; SES29879.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9W7Y1; -.
DR STRING; 641238.SAMN04490244_109173; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000198885; Unassembled WGS sequence.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd02790; MopB_CT_Formate-Dh_H; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041925; CT_Formate-Dh_H.
DR InterPro; IPR041924; Formate_Dh-H_N.
DR InterPro; IPR006478; Formate_DH_asu.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000198885};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 4..84
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 143..173
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 182..215
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 228..283
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 928 AA; 100870 MW; FB9DAB9E14DB8DEE CRC64;
MTDDTIRITL DGRQVEAAPG ETLWQVAKRH GTTIPHLCHR DAPGYRPDGN CRACMVSVEG
ERNLVASCIR QAQDGMEVTT EGTREVEARR LVMELLLADQ PARSEAHDAS AHIWDMAAAQ
GIRESRFPAL EPDRVPLLDD SHVAMSVNLD ACIQCNLCVR ACREVQVNDV IGMADRGHDA
YPVFDFDDPM GESTCVACGE CVQACPTGAL MPSSIMDSEQ RGDRADYDEE VDSVCPFCGV
GCQVSLKVKD DRIAYVQGID GPANEGRLCV KGRFGFDYIH SPERLTVPLI RREDAPPKGL
NVDPANPWTH FREATWDEAL KAAATGLAGL RDAHGGRSVA GFGSAKCTNE EAYLFQKLIR
TGFGHNNVDH CTRLCHASSV AALQENVGSG AVTAGFNEIE NADVAIVIGA NPTENHPVAA
TYFKQFAKRG GELIVIDPRG QALKRHASHM LQFRPGTDVA LLNAIMHVIV EEGLHDRQYI
DGFTDGFEGF RAHIAGFDPE RMSEICGIDA ETIRTVARVF AGAQRGMIFW GMGVSQHIHG
TDNARCLIAL ALLCGHVGRP GTGLHPLRGQ NNVQGASDAG LIPMVMPDYA SVMDDEVRAL
YRDLWGGTEI DPQPGLTVVE IVEAMHARQI RGMYILGENP AMSDPDVEHA RDGLAMLDHL
VVQDIFLTET AMFADVILPA AAFPEKTGTV TNTNRQVQMG RRAVPAPGQA REDWRIVVDL
ARQLGLDWSY ADPSEIFAEM TRAMPSLDNI TWDRLVTEGA VQYPCPSPNS PGESVVFGDG
FPRADGRALF APARVTPPAE TPDEDFPMIL TTGRQLEHWH TGAMTRRATV LDAMEPGATC
SLHPSTLRRL GVVAGDKVRL TTRRGSLEVA TRSDRAVSPD MVFLPFAYVE AAANILTNAA
LDPYGKIPEF KYSAVRVESA GAEELAAE
//
