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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
 
 
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