ID YQAB_ECOLI Reviewed; 188 AA.
AC P77475;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 12-APR-2017, entry version 129.
DE RecName: Full=Fructose-1-phosphate phosphatase YqaB;
DE EC=3.1.3.-;
DE AltName: Full=Fructose-1-phosphatase;
GN Name=yqaB; OrderedLocusNames=b2690, JW2665;
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=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
RA Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT analysis of its sequence features.";
RL DNA Res. 4:91-113(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.,
RA Mau B., 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
RT MG1655 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
RT new 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.,
RA Arrowsmith C.H., Koonin E.V., Edwards A.M., Yakunin A.F.;
RT "Genome-wide analysis of substrate specificities of the Escherichia
RT coli haloacid dehalogenase-like phosphatase family.";
RL J. Biol. Chem. 281:36149-36161(2006).
CC -!- FUNCTION: Catalyzes strongly the dephosphorylation of fructose-1-
CC phosphate (Fru1P) and slightly the dephosphorylation of 6-
CC phosphogluconate (6P-Glu). It has low beta-phosphoglucomutase
CC activity. {ECO:0000269|PubMed:15808744,
CC 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
CC manganese, cobalt or zinc. {ECO:0000269|PubMed:16990279};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 mM for Fru1P (with magnesium ions as cofactor and at pH 9)
CC {ECO:0000269|PubMed:16990279};
CC KM=3.9 mM for 6P-Glu (with magnesium ions as cofactor and at pH
CC 9) {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; U00096; AAC75737.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16557.1; -; Genomic_DNA.
DR PIR; C65049; C65049.
DR RefSeq; NP_417175.1; NC_000913.3.
DR RefSeq; WP_000273290.1; NZ_LN832404.1.
DR ProteinModelPortal; P77475; -.
DR SMR; P77475; -.
DR BioGrid; 4262273; 22.
DR DIP; DIP-12842N; -.
DR IntAct; P77475; 5.
DR MINT; MINT-1265616; -.
DR STRING; 511145.b2690; -.
DR EPD; P77475; -.
DR PaxDb; P77475; -.
DR PRIDE; P77475; -.
DR DNASU; 945776; -.
DR EnsemblBacteria; AAC75737; AAC75737; b2690.
DR EnsemblBacteria; BAA16557; BAA16557; BAA16557.
DR GeneID; 945776; -.
DR KEGG; ecj:JW2665; -.
DR KEGG; eco:b2690; -.
DR PATRIC; 32120774; VBIEscCol129921_2784.
DR EchoBASE; EB3301; -.
DR EcoGene; EG13530; yqaB.
DR eggNOG; ENOG4107VXZ; Bacteria.
DR eggNOG; COG0637; LUCA.
DR HOGENOM; HOG000248341; -.
DR InParanoid; P77475; -.
DR OMA; CAQRMGI; -.
DR PhylomeDB; P77475; -.
DR BioCyc; EcoCyc:G7408-MONOMER; -.
DR BioCyc; MetaCyc:G7408-MONOMER; -.
DR PRO; PR:P77475; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008801; F:beta-phosphoglucomutase activity; IDA:EcoliWiki.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; IDA:EcoCyc.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR010976; B-phosphoglucomutase_hydrolase.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023198; PGP_dom2.
DR Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
DR TIGRFAMs; TIGR02009; PGMB-YQAB-SF; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1 188 Fructose-1-phosphate phosphatase YqaB.
FT /FTId=PRO_0000108063.
FT REGION 11 13 Substrate binding. {ECO:0000250}.
FT ACT_SITE 11 11 Nucleophile. {ECO:0000250}.
FT METAL 11 11 Magnesium. {ECO:0000250}.
FT METAL 13 13 Magnesium. {ECO:0000250}.
FT METAL 167 167 Magnesium. {ECO:0000250}.
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CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 8 183 ipfam:HAD_2 [T]
SQ SEQUENCE 188 AA; 20780 MW; AA3F9FF1DF3B2024 CRC64;
MYERYAGLIF DMDGTILDTE PTHRKAWREV LGHYGLQYDI QAMIALNGSP TWRIAQAIIE
LNQADLDPHA LAREKTEAVR SMLLDSVEPL PLVDVVKSWH GRRPMAVGTG SESAIAEALL
AHLGLRHYFD AVVAADHVKH HKPAPDTFLL CAQRMGVQPT QCVVFEDADF GIQAARAAGM
DAVDVRLL
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