FDNH_SHIFL
ID FDNH_SHIFL Reviewed; 294 AA.
AC P0AAJ4; P24184; P77166;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Formate dehydrogenase, nitrate-inducible, iron-sulfur subunit;
DE AltName: Full=Anaerobic formate dehydrogenase iron-sulfur subunit;
DE AltName: Full=Formate dehydrogenase-N subunit beta;
DE Short=FDH-N subunit beta;
GN Name=fdnH; OrderedLocusNames=SF1750, S1883;
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. The beta subunit FdnH is an electron transfer
CC unit containing 4 iron-sulfur clusters; it serves as a conduit for
CC electrons that are transferred from the formate oxidation site in the
CC alpha subunit (FdnG) to the menaquinone associated with the gamma
CC subunit (FdnI) of formate dehydrogenase-N. Formate dehydrogenase-N is
CC part of a system that generates proton motive force, together with the
CC dissimilatory nitrate reductase (Nar) (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P0AAJ3};
CC Note=Binds 4 [4Fe-4S] clusters per subunit.
CC {ECO:0000250|UniProtKB:P0AAJ3};
CC -!- SUBUNIT: Trimer of heterotrimers, consisting of subunits alpha, beta
CC and gamma. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}.
CC -!- INDUCTION: By nitrate under anaerobic conditions. {ECO:0000250}.
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DR EMBL; AE005674; AAN43322.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17208.1; -; Genomic_DNA.
DR RefSeq; NP_707615.1; NC_004337.2.
DR RefSeq; WP_001240582.1; NZ_WPGW01000120.1.
DR AlphaFoldDB; P0AAJ4; -.
DR SMR; P0AAJ4; -.
DR STRING; 198214.SF1750; -.
DR EnsemblBacteria; AAN43322; AAN43322; SF1750.
DR EnsemblBacteria; AAP17208; AAP17208; S1883.
DR GeneID; 1024947; -.
DR GeneID; 66674673; -.
DR KEGG; sfl:SF1750; -.
DR KEGG; sfx:S1883; -.
DR PATRIC; fig|198214.7.peg.2073; -.
DR HOGENOM; CLU_043374_0_3_6; -.
DR OMA; FCVDRIQ; -.
DR OrthoDB; 1762646at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
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:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045333; P:cellular respiration; IEA:InterPro.
DR GO; GO:0015944; P:formate oxidation; IEA:InterPro.
DR CDD; cd10558; FDH-N; 1.
DR Gene3D; 1.20.5.480; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR006470; Formate_DH_bsu_Proteobacteria.
DR InterPro; IPR038384; Formate_DH_C_sf.
DR InterPro; IPR014603; Formate_DH_Fe-S_su.
DR InterPro; IPR015246; Formate_DH_TM.
DR Pfam; PF13247; Fer4_11; 1.
DR Pfam; PF12800; Fer4_4; 1.
DR Pfam; PF09163; Form-deh_trans; 1.
DR PIRSF; PIRSF036298; FDH_4Fe4S; 1.
DR TIGRFAMs; TIGR01582; FDH-beta; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 4.
PE 3: Inferred from homology;
KW 4Fe-4S; Cell inner membrane; Cell membrane; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..294
FT /note="Formate dehydrogenase, nitrate-inducible, iron-
FT sulfur subunit"
FT /id="PRO_0000159248"
FT TOPO_DOM 1..256
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 257..279
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 280..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 30..58
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 91..123
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 124..153
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 158..189
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 39
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 42
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 45
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 100
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 103
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 108
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 112
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 133
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 136
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 139
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 143
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 160
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 163
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 175
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
FT BINDING 179
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AAJ3"
SQ SEQUENCE 294 AA; 32239 MW; 44F361F4AC0AEF36 CRC64;
MAMETQDIIK RSATNSITPP SQVRDYKAEV AKLIDVSTCI GCKACQVACS EWNDIRDEVG
HCVGVYDNPA DLSAKSWTVM RFSETEQNGK LEWLIRKDGC MHCEDPGCLK ACPSAGAIIQ
YANGIVDFQS ENCIGCGYCI AGCPFNIPRL NKEDNRVYKC TLCVDRVSVG QEPACVKTCP
TGAIHFGTKK EMLELAEQRV AKLKARGYEH AGVYNPEGVG GTHVMYVLHH ADQPELYHGL
PKDPKIDTSV SLWKGALKPL AAAGFIATFA GLIFHYIGIG PNKEVDDDEE DHHE
