YIEH_ECOLI
ID YIEH_ECOLI Reviewed; 221 AA.
AC P31467; Q2M833;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=6-phosphogluconate phosphatase;
DE EC=3.1.3.-;
GN Name=yieH; OrderedLocusNames=b3715, JW3693;
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=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
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 FUNCTION AS A PHOSPHATASE.
RX PubMed=15808744; DOI=10.1016/j.fmrre.2004.12.006;
RA Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A.,
RA Arrowsmith C.H., Edwards A.M., Yakunin A.F.;
RT "Enzyme genomics: application of general enzymatic screens to discover new
RT enzymes.";
RL FEMS Microbiol. Rev. 29:263-279(2005).
RN [5]
RP FUNCTION AS A PHOSPHATASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND COFACTOR.
RX PubMed=16990279; DOI=10.1074/jbc.m605449200;
RA Kuznetsova E., Proudfoot M., Gonzalez C.F., Brown G., Omelchenko M.V.,
RA Borozan I., Carmel L., Wolf Y.I., Mori H., Savchenko A.V., Arrowsmith C.H.,
RA Koonin E.V., Edwards A.M., Yakunin A.F.;
RT "Genome-wide analysis of substrate specificities of the Escherichia coli
RT haloacid dehalogenase-like phosphatase family.";
RL J. Biol. Chem. 281:36149-36161(2006).
CC -!- FUNCTION: Catalyzes strongly the dephosphorylation of 6-
CC phosphogluconate (6P-Glu) and slightly the dephosphorylation of
CC dihydroxyacetone phosphate (DHAP) and phosphoenolpyruvate (PEP). Also
CC hydrolyzes both purines (GMP and IMP) and pyrimidines as secondary
CC substrates. {ECO:0000269|PubMed:15808744, ECO:0000269|PubMed:16990279}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16990279};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16990279};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:16990279};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16990279};
CC Note=Magnesium. Can also use other divalent metal cations as manganese,
CC cobalt or zinc. {ECO:0000269|PubMed:16990279};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.2 mM for 6P-Glu (with magnesium ions as cofactor and at pH 9)
CC {ECO:0000269|PubMed:16990279};
CC KM=2.9 mM for PEP (with manganese ions as cofactor and at pH 9)
CC {ECO:0000269|PubMed:16990279};
CC pH dependence:
CC Optimum pH is between 6 and 7.5. {ECO:0000269|PubMed:16990279};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
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DR EMBL; L10328; AAA62066.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76738.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77573.1; -; Genomic_DNA.
DR PIR; D65174; D65174.
DR RefSeq; NP_418171.1; NC_000913.3.
DR RefSeq; WP_000086486.1; NZ_SSZK01000035.1.
DR AlphaFoldDB; P31467; -.
DR SMR; P31467; -.
DR BioGRID; 4263102; 8.
DR STRING; 511145.b3715; -.
DR PaxDb; P31467; -.
DR PRIDE; P31467; -.
DR DNASU; 948232; -.
DR EnsemblBacteria; AAC76738; AAC76738; b3715.
DR EnsemblBacteria; BAE77573; BAE77573; BAE77573.
DR GeneID; 948232; -.
DR KEGG; ecj:JW3693; -.
DR KEGG; eco:b3715; -.
DR PATRIC; fig|1411691.4.peg.2986; -.
DR EchoBASE; EB1676; -.
DR eggNOG; COG0637; Bacteria.
DR HOGENOM; CLU_045011_13_2_6; -.
DR InParanoid; P31467; -.
DR OMA; MDVYGFT; -.
DR PhylomeDB; P31467; -.
DR BioCyc; EcoCyc:EG11725-MON; -.
DR BioCyc; MetaCyc:EG11725-MON; -.
DR PRO; PR:P31467; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..221
FT /note="6-phosphogluconate phosphatase"
FT /id="PRO_0000108060"
FT ACT_SITE 10
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 10..12
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 221 AA; 24664 MW; C50CF0A788D7CE5F CRC64;
MSRIEAVFFD CDGTLVDSEV ICSRAYVTMF QEFGITLDPE EVFKRFKGVK LYEIIDIVSL
EHGVTLAKTE AEHVYRAEVA RLFDSELEAI EGAGALLSAI TAPMCVVSNG PNNKMQHSMG
KLNMLHYFPD KLFSGYDIQR WKPDPALMFH AAKAMNVNVE NCILVDDSVA GAQSGIDAGM
EVFYFCADPH NKPIVHPKVT TFTHLSQLPE LWKARGWDIT A
