ID E8XJ18_SALT4 Unreviewed; 1015 AA.
AC E8XJ18;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Formate dehydorgenase-N alpha subunit {ECO:0000313|EMBL:ADX17270.1};
GN Name=fdnG {ECO:0000313|EMBL:ADX17270.1};
GN OrderedLocusNames=STM474_1583 {ECO:0000313|EMBL:ADX17270.1};
OS Salmonella typhimurium (strain 4/74).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=909946 {ECO:0000313|EMBL:ADX17270.1, ECO:0000313|Proteomes:UP000008978};
RN [1] {ECO:0000313|EMBL:ADX17270.1, ECO:0000313|Proteomes:UP000008978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4/74 {ECO:0000313|Proteomes:UP000008978};
RX PubMed=21478351; DOI=10.1128/JB.00394-11;
RA Richardson E.J., Limaye B., Inamdar H., Datta A., Manjari K.S.,
RA Pullinger G.D., Thomson N.R., Joshi R.R., Watson M., Stevens M.P.;
RT "Genome sequences of Salmonella enterica serovar typhimurium, Choleraesuis,
RT Dublin, and Gallinarum strains of well- defined virulence in food-producing
RT animals.";
RL J. Bacteriol. 193:3162-3163(2011).
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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP002487; ADX17270.1; -; Genomic_DNA.
DR RefSeq; WP_010989019.1; NC_016857.1.
DR KEGG; seb:STM474_1583; -.
DR PATRIC; fig|909946.3.peg.1620; -.
DR HOGENOM; CLU_000422_1_2_6; -.
DR Proteomes; UP000008978; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0047111; F:formate dehydrogenase (cytochrome-c-553) activity; IEA:InterPro.
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:InterPro.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR CDD; cd02752; MopB_Formate-Dh-Na-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006443; Formate-DH-alph_fdnG.
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 InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR01553; formate-DH-alph; 1.
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 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; PS00932; MOLYBDOPTERIN_PROK_3; 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 Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Selenium {ECO:0000313|EMBL:ADX17270.1};
KW Selenocysteine {ECO:0000256|ARBA:ARBA00022933,
KW ECO:0000313|EMBL:ADX17270.1}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 43..106
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT NON_STD 196
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:ADX17270.1"
SQ SEQUENCE 1015 AA; 112917 MW; C3420A38BFB19B70 CRC64;
MDVSRRQFFK ICAGGMAGTT VAALGFTPKM ALAQARNYKL LRAKEIRNSC TYCSVGCGLL
MYSLGDGAKN AKEAIYHIEG DPDHPVSRGA LCPKGAGLLD YVHSEDRLRY PEYRAPGSDK
WQRISWDDAF TRIAKLMKAD RDANFIEKNE QGVTVNRWLS TGMLCASAAS NETGMLTQKF
ARSLGMLAVD NQARVUHGPT VASLAPTFGR GAMTNHWVDI KNANVVMVMG GNAAEAHPVG
FRWAMEAKNN NDATLIVVDP RFTRTASVAD IYAPIRSGTD ITFLSGVLLY LIENNKINAE
YVKHYTNASL LVRDDFAFDD GLFSGYDAQK RQYDKSSWNY QFDENGYAKR DETLTHPRCV
WNLLKQHVSR YTPDVVENIC GTPKADFLKV CEVLASTSVP DRTTTFLYAL GWTQHTVGAQ
NIRTMAMIQL LLGNMGMAGG GVNALRGHSN IQGLTDLGLL STSLPGYLTL PSEKQADLQT
YLAANTPKAT LADQVNYWGN YPKFFVSLMK SFYGDAAQQE NDWGFAWLPK WDQSYDVIKY
FNMMDSGKVT GYFCQGFNPV ASFPDKNKVV QSLSKLKYLV VIDPLVTETS TFWQNHGESN
DVDPTTIQTE VFRLPSTCFA EEDGSIANSG RWLQWHWKGQ DAPGEARNDG EILAGIYHRL
REMYRAEGGK GAEPLLKMSW NYKQPDEPHS EEVAKENNGY ALEDLYDANG TLLARKGQLL
SSFALLRDDG TTSSSCWIYT GSWTEQGNQM SRRDNADPSG LGNTLGWAWA WPLNRRVLYN
RASADPQGKP WDPKRMLIQW NGAKWTGNDI PDFNNAAPGS GTNPFIMQPE GLGRLFAIDK
MAEGPFPEHY EPMETPLGTN PLHPNVVSNP AARLYEEDAL RMGKKEQFPY VGTTYRLTEH
FHTWTKHALL NAIAQPEQFV EISETLAAAK GIANGDYVKV SSKRGFIRAV AVVTRRLRTL
HVNGQQVETV GIPIHWGFEG VARKGYIANT LTPNVGDANS QTPEYKAFLV NIEKA
//
