ID C3NKI5_SULIN Unreviewed; 979 AA.
AC C3NKI5;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN OrderedLocusNames=YN1551_0286 {ECO:0000313|EMBL:ACP47465.1};
OS Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=419942 {ECO:0000313|EMBL:ACP47465.1, ECO:0000313|Proteomes:UP000006818};
RN [1] {ECO:0000313|EMBL:ACP47465.1, ECO:0000313|Proteomes:UP000006818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y.N.15.51 / Yellowstone #2 {ECO:0000313|Proteomes:UP000006818};
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
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; CP001404; ACP47465.1; -; Genomic_DNA.
DR RefSeq; WP_012717049.1; NC_012623.1.
DR AlphaFoldDB; C3NKI5; -.
DR GeneID; 7810476; -.
DR KEGG; sin:YN1551_0286; -.
DR HOGENOM; CLU_000422_4_0_2; -.
DR Proteomes; UP000006818; Chromosome.
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:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd00207; fer2; 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; 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; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
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 Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 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; PS51839; 4FE4S_HC3; 1.
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}.
FT DOMAIN 4..80
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 80..120
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 138..168
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 182..210
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 257..313
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 979 AA; 108879 MW; 0AE413B412A560E6 CRC64;
MIFMSIKIAI DNKEIVANEG ETILSVLKRN GIYIPHICYN EGLVPIESCD SCLIEVNGKL
VRACSTRVKD GMNISVNSKR SMEARKNAIS RILRYHKLYC SMCENNNGDC VLHESVIKLN
INSQKYIEKP YQVDDSGPFY VYDPSQCILC GRCVEACQDF AVNEVIWINW DLNPPRVVWD
NGNPIGNSSC VNCGTCVTVC PVNALMEKSM VGEAGYLTWI NNDLKKKAIE AIGKAEDNFS
LLMTFSEIEA NARSSQIKKT KTVCIYCGVG CSFEVWTKGR KILKVEPKPE SPANGILTCV
KGKFGWDFVN SPERITKPLI REGDRFREAS WDEAISYIAK RLKEIKERYS PDSIGFIASD
KMSNEEAYLL QKLSRAVIGT NNVDNSARYC QAPATIGLWR TVGIGADSGT IKDIENANLI
IIVGHNTTES HPVIGSKVKR AKKIKGSKIV VIDVRKHEIA EKADLFIKPK PGTDAAVLAG
VTKYLIDQGW VDKEFIDKKV NGFEEFKESI KGFTLDYVES ITGVPREKIV KLAEIVHNAS
SVAVLWGMGV TQHLGGADTS TIISDLLLIT GNYGKPGSGA FPMRGHNNVQ GVSDFGCLPN
YLPGYQKLED ENIIGKFEEA WGVKLNRKAG LQIPQMIEGV LEGKIHALYI VGEDTVMVDC
GTPLTKQALE KVDFLVVQDM FMTETAKLAD VILPATASLE KDGTFVNTER RIQRFYKAME
PMGDSKPDWE IIQMVANALG ANWSYKHPAE IMDEIAKLCP IFAGVSYSRL EGFNSLLWPV
NEDGSDIPLL YTNAFATKDG KAILYPLTWK PPELKDEVHK VTVNTGRVLE HFHVGNMTRR
VEGLRRKVPE TFVEVSKELA SKYSIKDGDL VLVKSKFGGE IRARAIVSDR VEGEEIFIPL
YASDPSKGVN NLTGLVIDKA SGTPGYKDTP VVIEKIEEGK GGSPLPLDNW RFHVNERRRQ
IGIEVEKKWK REEFKPLTS
//
