ID Q8X5S0_ECO57 Unreviewed; 715 AA.
AC Q8X5S0; A0A0H3JIJ7; A0A6M0JCU9; Q7A916;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 6.
DT 27-MAR-2024, entry version 159.
DE SubName: Full=Formate dehydrogenase-H, selenopolypeptide subunit {ECO:0000313|EMBL:BAB38484.1};
GN Name=fdhF {ECO:0000313|EMBL:BAB38484.1};
GN ORFNames=ECs_5061 {ECO:0000313|EMBL:BAB38484.1};
OS Escherichia coli O157:H7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB38484.1, ECO:0000313|Proteomes:UP000000558};
RN [1] {ECO:0000313|EMBL:BAB38484.1, ECO:0000313|Proteomes:UP000000558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC {ECO:0000313|Proteomes:UP000000558};
RX PubMed=11258796; DOI=.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; BA000007; BAB38484.1; -; Genomic_DNA.
DR RefSeq; NP_313088.1; NC_002695.1.
DR RefSeq; WP_010904990.1; NZ_VOAI01000008.1.
DR STRING; 155864.Z5678; -.
DR GeneID; 914271; -.
DR KEGG; ecs:ECs_5061; -.
DR PATRIC; fig|386585.9.peg.5288; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_6; -.
DR Proteomes; UP000000558; Chromosome.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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:0045333; P:cellular respiration; IEA:UniProt.
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 Gene3D; 2.40.40.20; -; 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 Gene3D; 1.20.5.460; Single helix bin; 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 NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF000144; CbbBc; 2.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 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 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:UP000000558};
KW Selenium {ECO:0000313|EMBL:BAB38484.1};
KW Selenocysteine {ECO:0000313|EMBL:BAB38484.1}.
FT NON_STD 140
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:BAB38484.1"
SQ SEQUENCE 715 AA; 79404 MW; DBC9B372B19615ED CRC64;
MKKVVTVCPY CASGCKINLV VDNGKIVRAE AAQGKTNQGT LCLKGYYGWD FINDTQILTP
RLKTPMIRRQ RGGKLEPVSW DEALNYVAER LSAIKEKYGP DAIQTTGSSR GTGNETNYVM
QKFARAVIGT NNVDCCARVU HGPSVAGLHQ SVGNGAMSNA INEIDNTDLV FVFGYNPADS
HPIVANHVIN AKRNGAKIIV CDPRKIETAR IADMHIALKN GSNIALLNAM GHVIIEENLY
DKAFVASRTE GFEEYRKIVE GYTPESVEDI TGVSASEIRQ AARMYAQAKS AAILWGMGVT
QFYQGVETVR SLTSLAMLTG NLGKPHAGVN PVRGQNNVQG ACDMGALPDT YPGYQYVKDP
ANREKFAKAW GVESLPAHTG YRISELPHRA AHGEVRAAYI MGEDPLQTDA ELSAVRKAFE
DLELVIVQDI FMTKTASAAD VILPSTSWGE HEGVFTAADR GFQRFFKAVE PKWDLKTDWQ
IISEIATRMG YPMHYNNTQE IWDELRHLCP DFYGATYEKM GELGFIQWPC RDTSDADQGT
SYLFKEKFDT PNGLAQFFTC DWVAPIDKLT DEYPMVLSTV REVGHYSCRS MTGNCAALAA
LADEPGYAQI NTEDAKRLSI EDEALVWVHS RKGKIITRAQ VSDRPNKGAI YMTYQWWIGA
CNELVTENLS PITKTPEYKY CAVRVEPIAD QRAAEQYVID EYNKLKTRLR EAALA
//
