ID A0A4Y6N8X3_SALET Unreviewed; 715 AA. AC A0A4Y6N8X3; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 07-APR-2021, entry version 12. DE RecName: Full=Formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128}; DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128}; GN ORFNames=D4X88_19235 {ECO:0000313|EMBL:EBS6379395.1}, DQC01_11785 GN {ECO:0000313|EMBL:EBW7075619.1}, EGU88_20455 GN {ECO:0000313|EMBL:EBZ8334835.1}, EO194_19010 GN {ECO:0000313|EMBL:ECA7156660.1}, EO253_20400 GN {ECO:0000313|EMBL:ECA7102765.1}, EUV76_17970 GN {ECO:0000313|EMBL:ECB0585833.1}, GNC04_003811 GN {ECO:0000313|EMBL:HAE3817943.1}; OS Salmonella enterica subsp. enterica serovar Indiana. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=286783 {ECO:0000313|EMBL:EBW7075619.1}; RN [1] {ECO:0000313|EMBL:HAE3817943.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DMS 3702 {ECO:0000313|EMBL:HAE3817943.1}; RX PubMed=30286803; RA Souvorov A., Agarwala R., Lipman D.J.; RT "SKESA: strategic k-mer extension for scrupulous assemblies."; RL Genome Biol. 19:153-150(2018). RN [2] {ECO:0000313|EMBL:EBW7075619.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=382836 {ECO:0000313|EMBL:EBW7075619.1}, 553265 RC {ECO:0000313|EMBL:ECB0585833.1}, 599586 RC {ECO:0000313|EMBL:EBS6379395.1, ECO:0000313|Proteomes:UP000336314}, RC 636274 {ECO:0000313|EMBL:EBZ8334835.1}, 659381 RC {ECO:0000313|EMBL:ECA7156660.1}, and 661039 RC {ECO:0000313|EMBL:ECA7102765.1}; RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:HAE3817943.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DMS 3702 {ECO:0000313|EMBL:HAE3817943.1}; RG NCBI Pathogen Detection Project; RL Submitted (JUL-2018) 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: Belongs to the prokaryotic molybdopterin-containing CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EBW7075619.1}. 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; AAGWDL010000022; EBS6379395.1; -; Genomic_DNA. DR EMBL; AAHJAA010000044; EBW7075619.1; -; Genomic_DNA. DR EMBL; AAHSKH010000021; EBZ8334835.1; -; Genomic_DNA. DR EMBL; AAHVGF010000025; ECA7102765.1; -; Genomic_DNA. DR EMBL; AAHVFQ010000026; ECA7156660.1; -; Genomic_DNA. DR EMBL; AAHWIV010000022; ECB0585833.1; -; Genomic_DNA. DR EMBL; DAARSZ010000025; HAE3817943.1; -; Genomic_DNA. DR Proteomes; UP000336314; Unassembled WGS sequence. DR GO; GO:0009326; C:formate dehydrogenase complex; IEA:UniProtKB-EC. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro. 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; cd02790; MopB_CT_Formate-Dh_H; 1. DR CDD; cd02753; MopB_Formate-Dh-H; 1. 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 Pfam; PF04879; Molybdop_Fe4S4; 1. DR Pfam; PF00384; Molybdopterin; 1. DR Pfam; PF01568; Molydop_binding; 1. DR SMART; SM00926; Molybdop_Fe4S4; 1. DR SUPFAM; SSF50692; SSF50692; 1. DR TIGRFAMs; TIGR01591; Fdh-alpha; 1. DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1. DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1. DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1. DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1. PE 3: Inferred from homology; KW Iron {ECO:0000256|ARBA:ARBA00023004}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Molybdenum {ECO:0000256|ARBA:ARBA00022505}; KW NAD {ECO:0000256|ARBA:ARBA00023027}; KW Oxidoreductase {ECO:0000313|EMBL:EBW7075619.1}; KW Selenium {ECO:0000313|EMBL:EBW7075619.1}; KW Selenocysteine {ECO:0000313|EMBL:EBW7075619.1}. FT DOMAIN 1..56 FT /note="4Fe-4S Mo/W bis-MGD-type" FT /evidence="ECO:0000259|PROSITE:PS51669" FT NON_STD 140 FT /note="Selenocysteine" FT /evidence="ECO:0000313|EMBL:EBW7075619.1" SQ SEQUENCE 715 AA; 79212 MW; 159AF3532CF6B49F CRC64; MKKVVTVCPY CASGCKINLV VDNGKIVRAE AAQGKTNQGT LCLKGYYGWD FINDTQILTP RLKTPMIRRQ RGGKLESVSW DEALNYVAER LSAIKAKYGP DAIQTTGSSR GTGNETNYVM QKFARAVIGT NNVDCCARVU HGPSVAGLHQ SVGNGAMSNA INEIDNTDLV FVFGYNPADS HPIVANHVIN AKRNGAKIIV CDPRKIETAR IADMHIALKN GSNIALLNAM GHVIIEENLY DKAFVASRTE GFEEYSKIVE GYTPESVEEI TGVSAQEIRQ AARMYASAKS AAILWGMGVT QFYQGVETVR SLTSLAMLTG NLGKPSAGVN PVRGQNNVQG ACDMGALPDT YPGYQYVKFP ENREKFAKAW GVESLPAHTG YRISELPHRA AHGEVRAAYI MGEDPLQTDA ELSAVRKAFE DLELVIVQDI FMTKTASAAD VILPSTSWGE HEGVFSAADR GFQRFFKAVE PKWDLKTDWQ IISEIATRMG YPMHYNNTQE IWDELRHLCP DFYGATYEKM GELGYIQWPC RDTSDADQGT SYLFKEKFDT PNGLAQFFTC DWVAPIDKLT EEYPMVLSTV REVGHYSCRS MTGNCAALAA LADEPGYAQI NTADAARLGI EDEALVWVHS RKGKIITRAQ VSDRPNKGAI YMTYQWWIGA CNELVTENLS PITKTPEYKY CAVRVEPIAD QRAAEQYVID EYNKLKTRLR ESAMG //