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Entry: YEAD_ECOLI
LinkDB: YEAD_ECOLI
Original site: YEAD_ECOLI 
ID   YEAD_ECOLI              Reviewed;         294 AA.
AC   P39173; P76233; P76913;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   24-JAN-2024, entry version 146.
DE   RecName: Full=Putative glucose-6-phosphate 1-epimerase {ECO:0000250|UniProtKB:Q03161};
DE            EC=5.1.3.15 {ECO:0000250|UniProtKB:Q03161};
DE   AltName: Full=Putative D-hexose-6-phosphate mutarotase {ECO:0000250|UniProtKB:Q03161};
DE   AltName: Full=Unknown protein from 2D-page spots T26/PR37;
GN   Name=yeaD; Synonyms=yzzQ; OrderedLocusNames=b1780, JW1769;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
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   PROTEIN SEQUENCE OF 1-12.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded in the
RT   genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [5]
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   [6]
RP   CRYSTALLIZATION, AND SUBUNIT.
RX   PubMed=20693678; DOI=10.1107/s1744309110024140;
RA   You W., Qiu X., Zhang Y., Ma J., Gao Y., Zhang X., Niu L., Teng M.;
RT   "Crystallization and preliminary X-ray diffraction analysis of the putative
RT   aldose 1-epimerase YeaD from Escherichia coli.";
RL   Acta Crystallogr. F 66:951-953(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate;
CC         Xref=Rhea:RHEA:16249, ChEBI:CHEBI:58225, ChEBI:CHEBI:58247;
CC         EC=5.1.3.15; Evidence={ECO:0000250|UniProtKB:Q03161};
CC   -!- SUBUNIT: Monomer in solution. {ECO:0000269|PubMed:20693678}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate 1-epimerase family.
CC       {ECO:0000305}.
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DR   EMBL; U00096; AAC74850.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15577.1; -; Genomic_DNA.
DR   PIR; D64938; D64938.
DR   RefSeq; NP_416294.4; NC_000913.3.
DR   RefSeq; WP_001335909.1; NZ_SSZK01000001.1.
DR   AlphaFoldDB; P39173; -.
DR   SMR; P39173; -.
DR   BioGRID; 4260309; 34.
DR   IntAct; P39173; 2.
DR   STRING; 511145.b1780; -.
DR   jPOST; P39173; -.
DR   PaxDb; 511145-b1780; -.
DR   EnsemblBacteria; AAC74850; AAC74850; b1780.
DR   GeneID; 946572; -.
DR   KEGG; ecj:JW1769; -.
DR   KEGG; eco:b1780; -.
DR   PATRIC; fig|511145.12.peg.1853; -.
DR   EchoBASE; EB2544; -.
DR   eggNOG; COG0676; Bacteria.
DR   HOGENOM; CLU_048345_4_1_6; -.
DR   InParanoid; P39173; -.
DR   OMA; TQALHSY; -.
DR   OrthoDB; 9790727at2; -.
DR   PhylomeDB; P39173; -.
DR   BioCyc; EcoCyc:G6966-MONOMER; -.
DR   PRO; PR:P39173; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0047938; F:glucose-6-phosphate 1-epimerase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006974; P:DNA damage response; IEP:EcoliWiki.
DR   CDD; cd09020; D-hex-6-P-epi_like; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR   InterPro; IPR025532; G6P_1-epimerase.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   PANTHER; PTHR11122; APOSPORY-ASSOCIATED PROTEIN C-RELATED; 1.
DR   PANTHER; PTHR11122:SF13; GLUCOSE-6-PHOSPHATE 1-EPIMERASE; 1.
DR   Pfam; PF01263; Aldose_epim; 1.
DR   PIRSF; PIRSF016020; PHexose_mutarotase; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Isomerase; Reference proteome.
FT   CHAIN           1..294
FT                   /note="Putative glucose-6-phosphate 1-epimerase"
FT                   /id="PRO_0000213036"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000250|UniProtKB:Q03161"
FT   ACT_SITE        267
FT                   /evidence="ECO:0000250|UniProtKB:Q03161"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q03161"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q03161"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q03161"
SQ   SEQUENCE   294 AA;  32666 MW;  ADACFE6D46F20957 CRC64;
     MIKKIFALPV IEQISPVLSR RKLDELDLIV VDHPQVKASF ALQGAHLLSW KPAGEEEVLW
     LSNNTPFKNG VAIRGGVPVC WPWFGPAAQQ GLPAHGFARN LPWTLKSHHE DADGVALTFE
     LTQSEETKKF WPHDFTLLAH FRVGKTCEID LESHGEFETT SALHTYFNVG DIAKVSVSGL
     GDRFIDKVND AKENVLTDGI QTFPDRTDRV YLNPQDCSVI NDEALNRIIA VGHQHHLNVV
     GWNPGPALSI SMGDMPDDGY KTFVCVETAY ASETQKVTKE KPAHLAQSIR VAKR
//
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