ID A0A0X8G4D9_9FLAO Unreviewed; 904 AA.
AC A0A0X8G4D9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:AMC09795.1};
GN ORFNames=Lupro_00305 {ECO:0000313|EMBL:AMC09795.1};
OS Lutibacter profundi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lutibacter.
OX NCBI_TaxID=1622118 {ECO:0000313|EMBL:AMC09795.1, ECO:0000313|Proteomes:UP000059672};
RN [1] {ECO:0000313|Proteomes:UP000059672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP1 {ECO:0000313|Proteomes:UP000059672};
RA Wissuwa J., Le Moine Bauer S., Stokke R., Dahle H., Steen I.H.;
RT "Complete genome sequence of Lutibacter profundus strain LP1.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMC09795.1, ECO:0000313|Proteomes:UP000059672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP1 {ECO:0000313|EMBL:AMC09795.1,
RC ECO:0000313|Proteomes:UP000059672};
RX PubMed=27118569; DOI=10.1099/ijsem.0.001105;
RA Le Moine Bauer S., Roalkvam I., Steen I.H., Dahle H.;
RT "Lutibacter profundi sp. nov., isolated from a deep-sea hydrothermal system
RT on the Arctic Mid-Ocean Ridge and emended description of the genus
RT Lutibacter.";
RL Int. J. Syst. Evol. Microbiol. 66:2671-2677(2016).
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};
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DR EMBL; CP013355; AMC09795.1; -; Genomic_DNA.
DR RefSeq; WP_068205513.1; NZ_CP013355.1.
DR AlphaFoldDB; A0A0X8G4D9; -.
DR STRING; 1622118.Lupro_00305; -.
DR KEGG; lut:Lupro_00305; -.
DR PATRIC; fig|1622118.3.peg.63; -.
DR OrthoDB; 9792592at2; -.
DR Proteomes; UP000059672; 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:InterPro.
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; cd00508; MopB_CT_Fdh-Nap-like; 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; 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; 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; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 4: Predicted;
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:UP000059672}.
FT DOMAIN 189..218
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 225..281
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 904 AA; 100857 MW; EB8A2BAA1A6844A1 CRC64;
MKAYINNTAY DFLQGETILE FVRRIEKNNN AIPTMCQDDR LENFGSCRVC SVEVAREKDG
ITKTMASCHT PIAERLYIYH NTEKIKRLRK NIVELVLTDY PADKIFPAKG KKATPFQETI
TQIGIPTIRY PKGENHLDIE PDTSHPYIKS DLSQCINCFR CVRACEEIQG EMILGMSGRG
FATNIIKGFD TSFNLSACVS CGACVQTCPT DALTDKFETK TLIADKTVRT TCTYCGVGCQ
LDVSVINGEI KGIQAPETAE VNEGHTCLKG RFAFQFYNHP DRLKEPLIKK NGKFEEVSWN
EAYDFITKKL ISIKNEYGAD AVGGISSSRA TNEENYLMQK MIRVAIGTNN IDGCARVCHA
PTAYGMQQAF GTGAATNSIE DLNQTDAIFL FGANPTEAHP VTGAKIKQLF MKGVTSIVVD
PVKTKLAKLA TYHLQLRPGT NVAILNMMAH YIIKEKLVNQ SFINQYTEFY KDFEAHVADL
DMSELEELTG VSKELVKKAA IAYASAERAM EFHGLGVTEH YQGSKTVMLL SNIAMMTGNI
GKNGAGLNPL RGQNNVQGAA DMGVQPHQGA GYMDVNNFEV QQYYAKKYGV DKMPEHEGLK
IPEMIDATLQ GKFKALWIMG EDTLMTDPNS NHIRKAFEKL DLLIVQELFM SATAEMADIV
LPAASYFEKN GTFTNGERRV QRVNKVIDSI GNCKSDGQIM IDMMHRLGYK QPTGQLYDAA
KIVEEIADVI PFMKGVTWEG LGKNGLQWPV KDDGTDTKML HINGNFKKGK GTFHHFDFEE
TPELVEHRKK FPFILTTARQ LEHYNSGTMT RRTENQLISS NDYLEINPLD AGKKDISEGD
AVRIFSDRGS VNIPVKLNYT VKPGIVRTTF HQPEIFINLI TGNVGDKETL TPEYKVVAVD
FEKI
//
