YDHR_ECOLI
ID YDHR_ECOLI Reviewed; 101 AA.
AC P0ACX3; P77225; Q2MB61;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Putative monooxygenase YdhR;
DE EC=1.-.-.-;
GN Name=ydhR; OrderedLocusNames=b1667, JW1657;
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 / MG1655 / ATCC 47076;
RX PubMed=9023191; DOI=10.1128/jb.179.4.1105-1111.1997;
RA Hensel M., Shea J.E., Baeumler A.J., Gleeson C., Blattner F.R.,
RA Holden D.W.;
RT "Analysis of the boundaries of Salmonella pathogenicity island 2 and the
RT corresponding chromosomal region of Escherichia coli K-12.";
RL J. Bacteriol. 179:1105-1111(1997).
RN [2]
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 [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 IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of JW1657 from Escherichia coli.";
RL Submitted (NOV-2004) to the PDB data bank.
RN [6]
RP STRUCTURE BY NMR, SUBUNIT, AND FUNCTION.
RX PubMed=16260765; DOI=10.1110/ps.051809305;
RA Revington M., Semesi A., Yee A., Shaw G.S.;
RT "Solution structure of the Escherichia coli protein ydhR: a putative mono-
RT oxygenase.";
RL Protein Sci. 14:3115-3120(2005).
CC -!- FUNCTION: May function as monooxygenase and play a role in the
CC metabolism of aromatic compounds. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16260765}.
CC -!- INTERACTION:
CC P0ACX3; P0A6Y8: dnaK; NbExp=3; IntAct=EBI-544817, EBI-542092;
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DR EMBL; U68703; AAB47943.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74737.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76495.1; -; Genomic_DNA.
DR PIR; C64924; C64924.
DR RefSeq; NP_416182.1; NC_000913.3.
DR RefSeq; WP_000212657.1; NZ_STEB01000003.1.
DR PDB; 1WD6; X-ray; 2.90 A; A/B=1-101.
DR PDB; 2ASY; NMR; -; A/B=1-101.
DR PDB; 2HIQ; X-ray; 2.00 A; A/B=2-101.
DR PDBsum; 1WD6; -.
DR PDBsum; 2ASY; -.
DR PDBsum; 2HIQ; -.
DR AlphaFoldDB; P0ACX3; -.
DR BMRB; P0ACX3; -.
DR SMR; P0ACX3; -.
DR BioGRID; 4263223; 14.
DR DIP; DIP-48270N; -.
DR IntAct; P0ACX3; 2.
DR STRING; 511145.b1667; -.
DR jPOST; P0ACX3; -.
DR PaxDb; P0ACX3; -.
DR PRIDE; P0ACX3; -.
DR EnsemblBacteria; AAC74737; AAC74737; b1667.
DR EnsemblBacteria; BAE76495; BAE76495; BAE76495.
DR GeneID; 66674440; -.
DR GeneID; 946177; -.
DR KEGG; ecj:JW1657; -.
DR KEGG; eco:b1667; -.
DR PATRIC; fig|1411691.4.peg.592; -.
DR EchoBASE; EB3710; -.
DR eggNOG; ENOG5032SAI; Bacteria.
DR HOGENOM; CLU_179942_0_0_6; -.
DR InParanoid; P0ACX3; -.
DR OMA; LWKIWTE; -.
DR PhylomeDB; P0ACX3; -.
DR BioCyc; EcoCyc:G6895-MON; -.
DR EvolutionaryTrace; P0ACX3; -.
DR PRO; PR:P0ACX3; -.
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 InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR014910; YdhR.
DR PANTHER; PTHR39169; PTHR39169; 1.
DR Pfam; PF08803; ydhR; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase; Reference proteome.
FT CHAIN 1..101
FT /note="Putative monooxygenase YdhR"
FT /id="PRO_0000013854"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:2HIQ"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:2HIQ"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:2HIQ"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:2HIQ"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:2HIQ"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:2HIQ"
FT HELIX 59..73
FT /evidence="ECO:0007829|PDB:2HIQ"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2HIQ"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:2ASY"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:2HIQ"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:2HIQ"
FT TURN 96..100
FT /evidence="ECO:0007829|PDB:2ASY"
SQ SEQUENCE 101 AA; 11288 MW; A8D41BD1D99B21C9 CRC64;
MATLLQLHFA FNGPFGDAMA EQLKPLAESI NQEPGFLWKV WTESEKNHEA GGIYLFTDEK
SALAYLEKHT ARLKNLGVEE VVAKVFDVNE PLSQINQAKL A
