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 03-AUG-2022, entry version 140.
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; Proteobacteria; 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; P39173; -.
DR PRIDE; P39173; -.
DR EnsemblBacteria; AAC74850; AAC74850; b1780.
DR EnsemblBacteria; BAA15577; BAA15577; BAA15577.
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 PhylomeDB; P39173; -.
DR BioCyc; EcoCyc:G6966-MON; -.
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:cellular response to DNA damage stimulus; 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 Pfam; PF01263; Aldose_epim; 1.
DR PIRSF; PIRSF016020; PHexose_mutarotase; 1.
DR SUPFAM; SSF74650; SSF74650; 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
