ID B9KF82_CAMLR Unreviewed; 940 AA.
AC B9KF82;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Formate dehydrogenase N, alpha subunit, selenocysteine-containing {ECO:0000313|EMBL:ACM63717.1};
DE EC=1.17.1.9 {ECO:0000313|EMBL:ACM63717.1};
GN Name=fdhF {ECO:0000313|EMBL:ACM63717.1};
GN OrderedLocusNames=Cla_0358 {ECO:0000313|EMBL:ACM63717.1};
OS Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=306263 {ECO:0000313|EMBL:ACM63717.1, ECO:0000313|Proteomes:UP000007727};
RN [1] {ECO:0000313|EMBL:ACM63717.1, ECO:0000313|Proteomes:UP000007727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM2100 / D67 / ATCC BAA-1060
RC {ECO:0000313|Proteomes:UP000007727};
RX PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT "The complete genome sequence and analysis of the human pathogen
RT Campylobacter lari.";
RL Foodborne Pathog. Dis. 5:371-386(2008).
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}.
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DR EMBL; CP000932; ACM63717.1; -; Genomic_DNA.
DR STRING; 306263.Cla_0358; -.
DR KEGG; cla:CLA_0358; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_1_1_7; -.
DR Proteomes; UP000007727; Chromosome.
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 CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 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 InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 3.
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; PS51318; TAT; 1.
PE 3: Inferred from homology;
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ACM63717.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007727};
KW Selenium {ECO:0000313|EMBL:ACM63717.1};
KW Selenocysteine {ECO:0000313|EMBL:ACM63717.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 44..100
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT NON_STD 176
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:ACM63717.1"
SQ SEQUENCE 940 AA; 106031 MW; E316D674DFB30D67 CRC64;
MALARRNFLK LAGIAGLGSA AFGSENKAIR AASEQEVANP YPDSKIVRTI CSICSAGCGI
KAEVQDGVWV RQENAIEHPI SQGSHCCKGI DQIDLTKSKQ RIKYPMKKEN GKWVRLTWEQ
AINEIGDKML EIRKENGPDS VMFLGSAKFN NQQAYYFRKF AAFWGTNNID HVARIUHSAT
VAGVANTWGY GAMTNHFGDV TKHSKMMIIF GANTAVANPI GFKHLLQAKD RNNAKLVVVD
PVFTKTAVHA DEYVRIRPGT DIALVYGMLH LIFKNGWEDK EIIKTRTYGV EEIKAEAAKW
TPEVVEDVTG VPAAQLEKIT RMLATIKPAT LFWALGITQH SVGSSNTRIL AILQLVLGNI
GKPGAGTNII RGHDNVQGAT DMGCLADTLP AYYGLDDNAW NHFANFWNVD REYLNSRFYS
KEWMHEKGFS LAKWWQGVLH EEKTYSNSPI RVLWVQGTGI TSMAHTVKIQ EALKKLDMIV
IAEPFVNEVA VLADRPDGIY IIPACTQFET EGYVTATNRA MQWRSQVVKP IYESKEDQEI
MFAFAKKFGF YKEYTRGMKM ELKDHKLVQT RDDNDDNFIW PDDATREMSN GLLSIGLRGI
SAERLRKHQQ NWEHFDPDTQ RGLGGEVKGE YYGLPWPCWD KQHPGTSIMW NTDIPYEEGG
MGFRNRFGLE HDGHSQLADE AFTPKGCKVK GGYPQITKEN IEKVFNIKLS DKEKELMGAS
WSTDISGIIL EKCREKSACC LGNARARMKV WEFADPIPLH REPIHSPRWD LVKKYPTWGD
QEKNFRVESK FISEQQKTDW SKEFPTIISS MRLVNLSGAG MLERTSKYLA AITPEMFANV
HPELALKYGI NDGDMMWIHS PQGTKIKVKC VHNHSVTPDR ICLPYNFAGI MQGVDLSYNY
PEGTKPYTIG ESSNTVTNYG FDINTQISEF NAGLCRLEKA
//
