YDHF_ECOLI
ID YDHF_ECOLI Reviewed; 298 AA.
AC P76187; Q2MB66; Q6BF80;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Oxidoreductase YdhF;
DE EC=1.-.-.-;
GN Name=ydhF; OrderedLocusNames=b1647, JW1639;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
RP SEQUENCE REVISION TO 247.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [3]
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 2-298 IN COMPLEX WITH NADP.
RX PubMed=14649299; DOI=10.1023/a:1026177202925;
RA Abergel C., Coutard B., Byrne D., Chenivesse S., Claude J.-B.,
RA Deregnaucourt C., Fricaux T., Gianesini-Boutreux C., Jeudy S., Lebrun R.,
RA Maza C., Notredame C., Poirot O., Suhre K., Varagnol M., Claverie J.-M.;
RT "Structural genomics of highly conserved microbial genes of unknown
RT function in search of new antibacterial targets.";
RL J. Struct. Funct. Genomics 4:141-157(2003).
CC -!- FUNCTION: May function as oxidoreductase. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC reductase 2 subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAT48134.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76490.1; -; Genomic_DNA.
DR PIR; A64922; A64922.
DR RefSeq; WP_000250656.1; NZ_SSZK01000001.1.
DR RefSeq; YP_025305.1; NC_000913.3.
DR PDB; 1OG6; X-ray; 2.80 A; A/B/C=2-298.
DR PDB; 1UR3; X-ray; 2.57 A; M=2-298.
DR PDBsum; 1OG6; -.
DR PDBsum; 1UR3; -.
DR AlphaFoldDB; P76187; -.
DR SMR; P76187; -.
DR BioGRID; 4263045; 22.
DR STRING; 511145.b1647; -.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR TCDB; 8.A.5.1.7; the voltage-gated k(+) channel Beta-subunit (kvBeta) family.
DR jPOST; P76187; -.
DR PaxDb; P76187; -.
DR PRIDE; P76187; -.
DR EnsemblBacteria; AAT48134; AAT48134; b1647.
DR EnsemblBacteria; BAE76490; BAE76490; BAE76490.
DR GeneID; 60900194; -.
DR GeneID; 946960; -.
DR KEGG; ecj:JW1639; -.
DR KEGG; eco:b1647; -.
DR PATRIC; fig|1411691.4.peg.612; -.
DR EchoBASE; EB3196; -.
DR eggNOG; COG4989; Bacteria.
DR HOGENOM; CLU_023205_8_0_6; -.
DR InParanoid; P76187; -.
DR OMA; VVYAWVM; -.
DR PhylomeDB; P76187; -.
DR BioCyc; EcoCyc:G6887-MON; -.
DR EvolutionaryTrace; P76187; -.
DR PRO; PR:P76187; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..298
FT /note="Oxidoreductase YdhF"
FT /id="PRO_0000070394"
FT ACT_SITE 55
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 158..159
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:14649299"
FT BINDING 209..220
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:14649299"
FT BINDING 263..264
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:14649299"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:1UR3"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:1UR3"
FT TURN 22..28
FT /evidence="ECO:0007829|PDB:1UR3"
FT HELIX 31..44
FT /evidence="ECO:0007829|PDB:1UR3"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1UR3"
FT TURN 55..59
FT /evidence="ECO:0007829|PDB:1UR3"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:1UR3"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1UR3"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:1UR3"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1UR3"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1OG6"
FT HELIX 103..117
FT /evidence="ECO:0007829|PDB:1UR3"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:1UR3"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:1UR3"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:1UR3"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:1UR3"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:1UR3"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:1UR3"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:1UR3"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1UR3"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:1UR3"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:1UR3"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:1UR3"
FT HELIX 224..236
FT /evidence="ECO:0007829|PDB:1UR3"
FT HELIX 242..251
FT /evidence="ECO:0007829|PDB:1UR3"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1UR3"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:1UR3"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:1UR3"
FT HELIX 282..293
FT /evidence="ECO:0007829|PDB:1UR3"
SQ SEQUENCE 298 AA; 33676 MW; 984DACC2C04A6D9F CRC64;
MVQRITIAPQ GPEFSRFVMG YWRLMDWNMS ARQLVSFIEE HLDLGVTTVD HADIYGGYQC
EAAFGEALKL APHLRERMEI VSKCGIATTA REENVIGHYI TDRDHIIKSA EQSLINLATD
HLDLLLIHRP DPLMDADEVA DAFKHLHQSG KVRHFGVSNF TPAQFALLQS RLPFTLATNQ
VEISPVHQPL LLDGTLDQLQ QLRVRPMAWS CLGGGRLFND DYFQPLRDEL AVVAEELNAG
SIEQVVYAWV LRLPSQPLPI IGSGKIERVR AAVEAETLKM TRQQWFRIRK AALGYDVP
