Entry sw:YQAB_ECOLI

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   30-NOV-2016, entry version 126.
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}.
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; ECOL316407:JW2665-MONOMER; -.
DR   BioCyc; MetaCyc:G7408-MONOMER; -.
DR   PRO; PR:P77475; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; -; 2.
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}.
CC   --------------------------------------------------------------------------
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
//