(data stored in ACNUC7421 zone)

SWISSPROT: A0A0H2ZK05_PSEAB

ID   A0A0H2ZK05_PSEAB        Unreviewed;       178 AA.
AC   A0A0H2ZK05;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 12.
DE   RecName: Full=D,D-heptose 1,7-bisphosphate phosphatase {ECO:0000256|PIRNR:PIRNR004682};
DE            EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR004682};
GN   OrderedLocusNames=PA14_00070 {ECO:0000313|EMBL:ABJ14962.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ14962.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ14962.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ14962.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR004682,
CC       ECO:0000256|SAAS:SAAS00377993}.
CC   -!- SIMILARITY: Belongs to the gmhB family.
CC       {ECO:0000256|PIRNR:PIRNR004682}.
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DR   EMBL; CP000438; ABJ14962.1; -; Genomic_DNA.
DR   RefSeq; WP_003142196.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZK05; -.
DR   EnsemblBacteria; ABJ14962; ABJ14962; PA14_00070.
DR   KEGG; pau:PA14_00070; -.
DR   KO; K03273; -.
DR   OMA; EHQICLE; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR023214; HAD-like_dom.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR004446; Heptose_bisP_phosphatase.
DR   InterPro; IPR006543; Histidinol-phos.
DR   PIRSF; PIRSF004682; GmhB; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
DR   TIGRFAMs; TIGR01656; Histidinol-ppas; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZK05.
DR   SWISS-2DPAGE; A0A0H2ZK05.
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR004682};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR004682,
KW   ECO:0000256|SAAS:SAAS00078086};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR004682,
KW   ECO:0000256|SAAS:SAAS00078030}.
FT   ACT_SITE      9      9       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR004682-1}.
FT   ACT_SITE     11     11       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR004682-1}.
FT   SITE         52     52       Stabilizes the phosphoryl group.
FT                                {ECO:0000256|PIRSR:PIRSR004682-3}.
FT   SITE        102    102       Contributes to substrate recognition.
FT                                {ECO:0000256|PIRSR:PIRSR004682-3}.
FT   SITE        103    103       Stabilizes the phosphoryl group.
FT                                {ECO:0000256|PIRSR:PIRSR004682-3}.
SQ   SEQUENCE   178 AA;  19114 MW;  D5D3476357925801 CRC64;
     MSRSLLILDR DGVINLDSDD YIKTLDEWIP IPSSIEAIAR LSQAGWTVAV ATNQSGIARG
     YYDLAVLEAM HARLRELVAE QGGEVGLIVY CPHGPDDGCD CRKPKPGMLR QIGKHYGVDL
     SGIWFVGDSI GDLEAARAVD CQPVLVKTGK GVRTLGKPLP EGTLIFDDLA AVASALLQ
//

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