ID Q5LT58_RUEPO Unreviewed; 926 AA.
AC Q5LT58;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN OrderedLocusNames=SPO1556 {ECO:0000313|EMBL:AAV94843.1};
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS pomeroyi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV94843.1, ECO:0000313|Proteomes:UP000001023};
RN [1] {ECO:0000313|EMBL:AAV94843.1, ECO:0000313|Proteomes:UP000001023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC {ECO:0000313|Proteomes:UP000001023};
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA Daugherty S.C., Deboy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT environment.";
RL Nature 432:910-913(2004).
RN [2] {ECO:0000313|EMBL:AAV94843.1, ECO:0000313|Proteomes:UP000001023}
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC {ECO:0000313|Proteomes:UP000001023};
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV94843.1; -; Genomic_DNA.
DR RefSeq; WP_011047293.1; NC_003911.12.
DR AlphaFoldDB; Q5LT58; -.
DR STRING; 246200.SPO1556; -.
DR PaxDb; 246200-SPO1556; -.
DR KEGG; sil:SPO1556; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_5; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000001023; Chromosome.
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 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; 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 Oxidoreductase {ECO:0000313|EMBL:AAV94843.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001023}.
FT DOMAIN 8..88
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 145..175
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 188..217
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 230..285
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 926 AA; 100226 MW; 1D36260C376D51E7 CRC64;
MADGAHVEMV SFTLNGEEVT VPEGLTIWEA AHGRGLVIPH LCHKPDPGYR PDGNCRACMV
EVAGERTLVA SCIRPVAAGM VVTTDSARAE GARKMVVELL LADQPEVAHD ASSHFHAMAG
LNGVSESRFP ARDAAHVPLL DASHVAMRVN LDACINCNLC VRACREVQVN DVIGMAGRGA
GAQVVFDQND PMGASTCVAC GECVQACPTG ALMPATVLDA EQAGDSKDYD REVTSVCPFC
GVGCQLSFKV KDNKIKYVTG VDGPANESRL CVKGRFGFDY IDHPHRLTKP LIRRADAPKG
LNVDPGNPLS HFREASWEEA LDFAARGLAD LRAQKGSYVA GFGSAKCSNE EAYLFQKLIR
QGFGHNNVDH CTRLCHASSV SALLENVGSG AVTATFNEIE NADVAIVIGC NPIENHPVAA
TYFKQFTKRG GKLIVCDPRG VGMGRFATHR LQFKPGADVS MLNAMMHVIV EEGLYDQAYI
DQFTENWEEM KAHLADYSPE KMEPICGIAA GELRDAARTF AAGKAGMIFW GMGVSQHIHG
TDNSRCLISL ALMTGNVGKP GAGLHPLRGQ NNVQGASDAG LIPMFLPDYQ SVTDDGVRSA
FTSVWNSGDF SNQKGLTVVE IMHAIHDGDI RGMYILGENP AMSDPDVDHA RAALAMLEHL
VVQDIFLTET ANYADVILPA SAWAEKTGTV TNTNRQVQMG RPAVAPPGQA KEDWWIEVEL
ARRLGLDWNY SHPSEVFAEM KRNMKSLDNI TWARLEGEAV TYPSLSPEDP GQAIVFGDGF
PRANKRARFT PAKIVEPDER PDADYPFVLI TGRQLEHWHT GSMTRRASVL DAVEPEANCS
MHPATLRAMG IEPGDMIRLT TRRGSVQVMV RADRAIAQDN VFLPFAYVEA AANILTNAAL
DPYGKIPEFK YAAVKVERTD TAASAV
//
