(data stored in SCRATCH zone)

SWISSPROT: B7UJA2_ECO27

ID   B7UJA2_ECO27            Unreviewed;       190 AA.
AC   B7UJA2;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=D,D-heptose 1,7-bisphosphate phosphatase {ECO:0000256|PIRNR:PIRNR004682};
DE            EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR004682};
GN   Name=gmhB {ECO:0000313|EMBL:CAS07754.1};
GN   OrderedLocusNames=E2348C_0206 {ECO:0000313|EMBL:CAS07754.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07754.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07754.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR004682-4};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR004682-4};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR004682,
CC       ECO:0000256|SAAS:SAAS00078038}.
CC   -!- SIMILARITY: Belongs to the gmhB family.
CC       {ECO:0000256|PIRNR:PIRNR004682}.
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DR   EMBL; FM180568; CAS07754.1; -; Genomic_DNA.
DR   RefSeq; WP_001140167.1; NC_011601.1.
DR   SMR; B7UJA2; -.
DR   EnsemblBacteria; CAS07754; CAS07754; E2348C_0206.
DR   KEGG; ecg:E2348C_0206; -.
DR   HOGENOM; HOG000016501; -.
DR   KO; K03273; -.
DR   OMA; EHQICLE; -.
DR   BioCyc; ECOL574521:E2348C_RS01060-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR004446; Heptose_bisP_phosphatase.
DR   InterPro; IPR006543; Histidinol-phos.
DR   PANTHER; PTHR42891; PTHR42891; 1.
DR   PIRSF; PIRSF004682; GmhB; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR00213; GmhB_yaeD; 1.
DR   TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
DR   TIGRFAMs; TIGR01656; Histidinol-ppas; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UJA2.
DR   SWISS-2DPAGE; B7UJA2.
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR004682};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR004682,
KW   ECO:0000256|SAAS:SAAS00455224};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR004682,
KW   ECO:0000256|SAAS:SAAS00455242};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR004682-4};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR004682-4,
KW   ECO:0000256|SAAS:SAAS00863697};
KW   Zinc {ECO:0000256|PIRSR:PIRSR004682-4}.
FT   REGION       11     13       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR004682-2}.
FT   REGION       19     22       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR004682-2}.
FT   REGION       53     56       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR004682-2}.
FT   REGION      110    111       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR004682-2}.
FT   ACT_SITE     11     11       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR004682-1}.
FT   ACT_SITE     13     13       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR004682-1}.
FT   METAL        11     11       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR004682-4}.
FT   METAL        13     13       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR004682-4}.
FT   METAL        92     92       Zinc. {ECO:0000256|PIRSR:PIRSR004682-4}.
FT   METAL        94     94       Zinc; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR004682-4}.
FT   METAL       107    107       Zinc. {ECO:0000256|PIRSR:PIRSR004682-4}.
FT   METAL       109    109       Zinc. {ECO:0000256|PIRSR:PIRSR004682-4}.
FT   METAL       136    136       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR004682-4}.
FT   METAL       137    137       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR004682-4}.
FT   BINDING     137    137       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR004682-2}.
FT   SITE         53     53       Stabilizes the phosphoryl group.
FT                                {ECO:0000256|PIRSR:PIRSR004682-3}.
FT   SITE        110    110       Contributes to substrate recognition.
FT                                {ECO:0000256|PIRSR:PIRSR004682-3}.
FT   SITE        111    111       Stabilizes the phosphoryl group.
FT                                {ECO:0000256|PIRSR:PIRSR004682-3}.
SQ   SEQUENCE   190 AA;  21145 MW;  3313858A1128FA74 CRC64;
     MAKSVPAIFL DRDGTINVDH GYVHEIDNFE FIDGVIDAMR ELKKMGFALV VVTNQSGIAR
     GKFTEAQFET LTEWMDWSLA DRDVDLDGIY YCPHHPQGSV EEFRQVCDCR KPHPGMFLSA
     RDYLHIDMAA SYMVGDKLED MQAAAAASVG TKVLVRTGKP ITPEAENAAD WVLNSLADLP
     QAIKKQQKPA
//

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