ID A0A1H5U775_9RHOB Unreviewed; 929 AA.
AC A0A1H5U775;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=SAMN04488045_0891 {ECO:0000313|EMBL:SEF70962.1};
OS Thalassococcus halodurans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassococcus.
OX NCBI_TaxID=373675 {ECO:0000313|EMBL:SEF70962.1, ECO:0000313|Proteomes:UP000236752};
RN [1] {ECO:0000313|EMBL:SEF70962.1, ECO:0000313|Proteomes:UP000236752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26915 {ECO:0000313|EMBL:SEF70962.1,
RC ECO:0000313|Proteomes:UP000236752};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNUZ01000001; SEF70962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5U775; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000236752; 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; SSF50692; ADC-like; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 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:UP000236752};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 3..83
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 142..172
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 181..214
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 227..282
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 929 AA; 102861 MW; B724484963B4625D CRC64;
MSDTIRFILD GEEVEAQKGD TIWEVANGRG LKIPHLCHRP EPGYRPDGNC RACMVEIEGE
RTLAASCIRE PQEGMVVTTQ SNRAKTARKM VMELLVADQP EREVAHDKSS HFWDMADLNG
VTESRFPSMD AERIPLLDDS HVAMRVNLDA CIQCNLCVRA CREVQVNDVI GMADRGHDAF
PVFDLDDPMG ASSCVACGEC VQACPTGALM PASILDDQQQ GDRNDFDSEV KSICPFCGVG
CQVSIKVKDD KVAYVEGING PSNEGRLCVK GRFGFDYIHH GHRLTKPLIR RDDAPEKGLN
VDPSNPWTHF REATWEEALD FAAKGLVDLR SYYGGKSVAG FGSAKCTNEE AYLFQKLIRQ
GFKHNNVDHC TRLCHASSVA ALMENVGSGA VTASFNEIEN ADVAIVIGAN PTENHPVAAT
YFKQFTKRGG ELIIMDPRGQ NGLKRHAAYN LQFRPGMDVA LLNAIMNVIV EEKLYDRQYI
EGFTEGFFEF REHIRAFTPE RMAEICGIDA ETIRSVARTF ADARAAMIFW GMGVSQHVHG
TDNSRCLISL ALLCGHVGRP GTGLHPLRGQ NNVQGASDAG LIPHVMPDYQ SVADREVRDL
FRHIWRGTEI EETPGLTVVE IMDRVYRGEI RGMYVLGENP AMSDPDVDHA RKALAKLDHL
VVQDIFLTET ANYADVILPA SALPEKSGTV TNTNRQVQMV RRAVPTPGEA REDWEIVVDL
ARRIGLDWDY DDPREVFDEM KMSMRSLHHI TWKRLETESS VTYPCNGPED PGQAVVFGDG
FPRRAGRAKF TPARVTPPAE APDKDFPMVL TTGRQLEHWH TGSMTRRATV LDAVEPEANC
SIHPATLRQM GVEAGGRVRL TTRRGSVEIM ARADRNVAPD MVFLPFAYVE AAANILTNAA
LDPFGKIPEF KYSAVRVEAA DQPARVAAE
//
