FDNH_ECOLI
ID FDNH_ECOLI Reviewed; 294 AA.
AC P0AAJ3; P24184; P77166;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=b1475, JW1471;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1834669; DOI=10.1016/s0021-9258(18)54583-x;
RA Berg B.L., Li J., Heider J., Stewart V.;
RT "Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I.
RT Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA)
RT encodes selenocysteine.";
RL J. Biol. Chem. 266:22380-22385(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=2168848; DOI=10.1093/genetics/125.4.691;
RA Berg B.L., Stewart V.;
RT "Structural genes for nitrate-inducible formate dehydrogenase in
RT Escherichia coli K-12.";
RL Genetics 125:691-702(1990).
RN [6] {ECO:0007744|PDB:1KQF, ECO:0007744|PDB:1KQG}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH ALPHA AND GAMMA
RP SUBUNITS AND [4FE-4S] CLUSTERS, FUNCTION, COFACTOR, ELECTRON TRANSFER
RP CHAIN, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=11884747; DOI=10.1126/science.1068186;
RA Jormakka M., Tornroth S., Byrne B., Iwata S.;
RT "Molecular basis of proton motive force generation: structure of formate
RT dehydrogenase-N.";
RL Science 295:1863-1868(2002).
CC -!- FUNCTION: Formate dehydrogenase allows E.coli to use formate as major
CC electron donor during anaerobic respiration, when nitrate is used as
CC electron acceptor. The beta subunit FdnH is an electron transfer unit
CC containing 4 iron-sulfur clusters; it serves as a conduit for electrons
CC that are transferred from the formate oxidation site in the alpha
CC subunit (FdnG) to the menaquinone associated with the gamma subunit
CC (FdnI) of formate dehydrogenase-N. Formate dehydrogenase-N is part of a
CC system that generates proton motive force, together with the
CC dissimilatory nitrate reductase (Nar). {ECO:0000269|PubMed:11884747}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:11884747};
CC Note=Binds 4 [4Fe-4S] clusters per subunit.
CC {ECO:0000269|PubMed:11884747};
CC -!- SUBUNIT: Trimer of heterotrimers, consisting of subunits alpha, beta
CC and gamma. {ECO:0000269|PubMed:11884747}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:11884747}; Single-pass membrane protein
CC {ECO:0000269|PubMed:11884747}.
CC -!- INDUCTION: By nitrate under anaerobic conditions.
CC {ECO:0000269|PubMed:2168848}.
CC -!- MISCELLANEOUS: The 4Fe-4S clusters from PubMed:11884747 are renumbered
CC in standard order.
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DR EMBL; M75029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00096; AAD13439.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15124.1; -; Genomic_DNA.
DR PIR; F64900; JS0629.
DR RefSeq; NP_415992.1; NC_000913.3.
DR RefSeq; WP_001240582.1; NZ_STEB01000053.1.
DR PDB; 1KQF; X-ray; 1.60 A; B=1-294.
DR PDB; 1KQG; X-ray; 2.80 A; B=1-294.
DR PDBsum; 1KQF; -.
DR PDBsum; 1KQG; -.
DR AlphaFoldDB; P0AAJ3; -.
DR SMR; P0AAJ3; -.
DR BioGRID; 4262901; 24.
DR ComplexPortal; CPX-1975; Formate dehydrogenase N complex.
DR DIP; DIP-35836N; -.
DR IntAct; P0AAJ3; 18.
DR STRING; 511145.b1475; -.
DR DrugBank; DB07918; 2-heptyl-4-hydroxyquinoline N-oxide.
DR TCDB; 5.A.3.2.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR jPOST; P0AAJ3; -.
DR PaxDb; P0AAJ3; -.
DR PRIDE; P0AAJ3; -.
DR EnsemblBacteria; AAD13439; AAD13439; b1475.
DR EnsemblBacteria; BAA15124; BAA15124; BAA15124.
DR GeneID; 66674673; -.
DR GeneID; 948794; -.
DR KEGG; ecj:JW1471; -.
DR KEGG; eco:b1475; -.
DR PATRIC; fig|1411691.4.peg.792; -.
DR EchoBASE; EB1210; -.
DR eggNOG; COG0437; Bacteria.
DR HOGENOM; CLU_043374_0_3_6; -.
DR InParanoid; P0AAJ3; -.
DR OMA; FCVDRIQ; -.
DR PhylomeDB; P0AAJ3; -.
DR BioCyc; EcoCyc:FDNH-MON; -.
DR BioCyc; MetaCyc:FDNH-MON; -.
DR BRENDA; 1.17.5.3; 2026.
DR EvolutionaryTrace; P0AAJ3; -.
DR PRO; PR:P0AAJ3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009326; C:formate dehydrogenase complex; IDA:EcoCyc.
DR GO; GO:0071575; C:integral component of external side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0036397; F:formate dehydrogenase (quinone) activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019645; P:anaerobic electron transport chain; IC:ComplexPortal.
DR GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
DR GO; GO:0015944; P:formate oxidation; IDA:EcoCyc.
DR GO; GO:0006788; P:heme oxidation; IC:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Cell inner membrane; Cell membrane;
KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..294
FT /note="Formate dehydrogenase, nitrate-inducible, iron-
FT sulfur subunit"
FT /id="PRO_0000159247"
FT TOPO_DOM 1..256
FT /note="Periplasmic"
FT TRANSMEM 257..279
FT /note="Helical"
FT TOPO_DOM 280..294
FT /note="Cytoplasmic"
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:0000269|PubMed:11884747"
FT BINDING 42
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11884747"
FT BINDING 45
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11884747"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11884747"
FT BINDING 100
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11884747"
FT BINDING 103
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11884747"
FT BINDING 108
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11884747"
FT BINDING 112
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:11884747"
FT BINDING 133
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:11884747"
FT BINDING 136
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:11884747"
FT BINDING 139
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:11884747"
FT BINDING 143
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11884747"
FT BINDING 160
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11884747"
FT BINDING 163
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11884747"
FT BINDING 175
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11884747"
FT BINDING 179
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11884747"
FT CONFLICT 101..102
FT /note="MH -> ID (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1KQF"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:1KQF"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:1KQF"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 189..205
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1KQF"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:1KQF"
FT TURN 229..232
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1KQF"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 248..254
FT /evidence="ECO:0007829|PDB:1KQF"
FT HELIX 257..279
FT /evidence="ECO:0007829|PDB:1KQF"
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