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DescriptionRecName: Full=Formate dehydrogenase, nitrate-inducible, cytochrome b556(Fdn) subunit; AltName: Full=Anaerobic formate dehydrogenase cytochrome b556 subunit; AltName: Full=Formate dehydrogenase-N subunit gamma; Short=FDH-N subunit gamma;
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MyHits synonymsFDNI_SHIFL , P0AEK9 , P24185 , P77513 , B10073F14343515E
match map segment
ipfam:Ni_hydr_CYTB  
Legends: 1, Iron (heme B 1 axial ligand); via tele nitrogen. {ECO:0000250}; 2, Iron (heme B 2 axial ligand); via tele nitrogen. {ECO:0000250}; 3, BINDING Menaquinone; via pros nitrogen. {ECO:0000250}; 4, TOPO_DOM Cytoplasmic. {ECO:0000250}; 5, TRANSMEM Helical. {ECO:0000250}; 6, TOPO_DOM Periplasmic. {ECO:0000250}.
ID   FDNI_SHIFL              Reviewed;         217 AA.
AC   P0AEK9; P24185; P77513;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   02-NOV-2016, entry version 82.
DE   RecName: Full=Formate dehydrogenase, nitrate-inducible, cytochrome b556(Fdn) subunit;
DE   AltName: Full=Anaerobic formate dehydrogenase cytochrome b556 subunit;
DE   AltName: Full=Formate dehydrogenase-N subunit gamma;
DE            Short=FDH-N subunit gamma;
GN   Name=fdnI; OrderedLocusNames=SF1749, S1882;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/IAI.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Formate dehydrogenase allows the bacterium to use
CC       formate as major electron donor during anaerobic respiration, when
CC       nitrate is used as electron acceptor. Subunit gamma is the
CC       cytochrome b556 component of the formate dehydrogenase-N, and also
CC       contains a menaquinone reduction site that receives electrons from
CC       the beta subunit (FdnH), through its hemes. Formate dehydrogenase-
CC       N is part of a system that generates proton motive force, together
CC       with the dissimilatory nitrate reductase (Nar) (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC       Note=Binds 2 heme groups per subunit. Heme 1 is located at the
CC       cytoplasmic interface, heme 2 is located at the periplasmic
CC       interface. Electrons are transferred from the periplasmic to the
CC       cytoplasmic heme. {ECO:0000250};
CC   -!- SUBUNIT: Trimer of heterotrimers, consisting of subunits alpha,
CC       beta and gamma. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the formate dehydrogenase gamma subunit
CC       family. {ECO:0000305}.
DR   EMBL; AE005674; AAN43321.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17207.1; -; Genomic_DNA.
DR   RefSeq; NP_707614.2; NC_004337.2.
DR   RefSeq; WP_000045648.1; NZ_LVJC01000105.1.
DR   ProteinModelPortal; P0AEK9; -.
DR   SMR; P0AEK9; -.
DR   STRING; 198214.SF1749; -.
DR   PaxDb; P0AEK9; -.
DR   PRIDE; P0AEK9; -.
DR   EnsemblBacteria; AAN43321; AAN43321; SF1749.
DR   EnsemblBacteria; AAP17207; AAP17207; S1882.
DR   GeneID; 1024930; -.
DR   KEGG; sfl:SF1749; -.
DR   KEGG; sft:NCTC1_01894; -.
DR   KEGG; sfx:S1882; -.
DR   PATRIC; 18705181; VBIShiFle31049_2086.
DR   eggNOG; ENOG4108MG3; Bacteria.
DR   eggNOG; COG2864; LUCA.
DR   HOGENOM; HOG000163500; -.
DR   KO; K08350; -.
DR   OMA; KQDIPWL; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0009326; C:formate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier 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:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR   InterPro; IPR011577; Cyt_b561_bac/Ni-Hgenase.
DR   InterPro; IPR016174; Di-haem_cyt_TM.
DR   InterPro; IPR006471; Formate_DH_gsu.
DR   Pfam; PF01292; Ni_hydr_CYTB; 1.
DR   SUPFAM; SSF81342; SSF81342; 1.
DR   TIGRFAMs; TIGR01583; formate-DH-gamm; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Complete proteome;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    217       Formate dehydrogenase, nitrate-inducible,
FT                                cytochrome b556(Fdn) subunit.
FT                                /FTId=PRO_0000087212.
FT   TOPO_DOM      1     11       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM     12     36       Helical. {ECO:0000250}.
FT   TOPO_DOM     37     52       Periplasmic. {ECO:0000250}.
FT   TRANSMEM     53     74       Helical. {ECO:0000250}.
FT   TOPO_DOM     75    110       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM    111    134       Helical. {ECO:0000250}.
FT   TOPO_DOM    135    150       Periplasmic. {ECO:0000250}.
FT   TRANSMEM    151    175       Helical. {ECO:0000250}.
FT   TOPO_DOM    176    217       Cytoplasmic. {ECO:0000250}.
FT   METAL        18     18       Iron (heme B 1 axial ligand); via tele
FT                                nitrogen. {ECO:0000250}.
FT   METAL        57     57       Iron (heme B 2 axial ligand); via tele
FT                                nitrogen. {ECO:0000250}.
FT   METAL       155    155       Iron (heme B 2 axial ligand); via tele
FT                                nitrogen. {ECO:0000250}.
FT   METAL       169    169       Iron (heme B 1 axial ligand); via tele
FT                                nitrogen. {ECO:0000250}.
FT   BINDING     169    169       Menaquinone; via pros nitrogen.
FT                                {ECO:0000250}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        13    186       ipfam:Ni_hydr_CYTB [T]
SQ   SEQUENCE   217 AA;  25368 MW;  B10073F14343515E CRC64;
     MSKSKMIVRT KFIDRACHWT VVICFFLVAL SGISFFFPTL QWLTQTFGTP QMGRILHPFF
     GIAIFVALMF MFVRFVHHNI PDKKDIPWLL NIVEVLKGNE HKVADVGKYN AGQKMMFWSI
     MSMIFVLLVT GVIIWRPYFA QYFPMQVVRY SLLIHAAAGI ILIHAILIHM YMAFWVKGSI
     KGMIEGKVSR RWAKKHHPRW YREIEKAEAK KESEEGI
//