FDNI_SHIFL
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 03-AUG-2022, entry version 110.
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., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., 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., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Formate dehydrogenase allows the bacterium to use formate as
CC major electron donor during anaerobic respiration, when nitrate is used
CC as electron acceptor. Subunit gamma is the cytochrome b556 component of
CC the formate dehydrogenase-N, and also contains a menaquinone reduction
CC site that receives electrons from the beta subunit (FdnH), through its
CC hemes. Formate dehydrogenase-N is part of a system that generates
CC proton motive force, together with the dissimilatory nitrate reductase
CC (Nar) (By similarity). {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 interface.
CC Electrons are transferred from the periplasmic to the cytoplasmic heme.
CC {ECO:0000250};
CC -!- SUBUNIT: Trimer of heterotrimers, consisting of subunits alpha, beta
CC and gamma. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the formate dehydrogenase gamma subunit family.
CC {ECO:0000305}.
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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_WPGW01000120.1.
DR AlphaFoldDB; P0AEK9; -.
DR SMR; P0AEK9; -.
DR STRING; 198214.SF1749; -.
DR EnsemblBacteria; AAN43321; AAN43321; SF1749.
DR EnsemblBacteria; AAP17207; AAP17207; S1882.
DR GeneID; 1024930; -.
DR GeneID; 66674672; -.
DR KEGG; sfl:SF1749; -.
DR KEGG; sfx:S1882; -.
DR PATRIC; fig|198214.7.peg.2072; -.
DR HOGENOM; CLU_091368_1_1_6; -.
DR OMA; TIMSMIF; -.
DR OrthoDB; 1612137at2; -.
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 transfer 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; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..217
FT /note="Formate dehydrogenase, nitrate-inducible, cytochrome
FT b556(Fdn) subunit"
FT /id="PRO_0000087212"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 37..52
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 53..74
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 75..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 111..134
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 135..150
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 151..175
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 176..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="a menaquinone"
FT /ligand_id="ChEBI:CHEBI:16374"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
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
