(data stored in SCRATCH zone)

SWISSPROT: Q500T8_PSEU2

ID   Q500T8_PSEU2            Unreviewed;       180 AA.
AC   Q500T8;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 85.
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=Psyr_0010 {ECO:0000313|EMBL:AAY35084.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35084.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35084.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35084.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY35084.1; -; Genomic_DNA.
DR   RefSeq; WP_003401440.1; NC_007005.1.
DR   RefSeq; YP_233122.1; NC_007005.1.
DR   STRING; 205918.Psyr_0010; -.
DR   EnsemblBacteria; AAY35084; AAY35084; Psyr_0010.
DR   GeneID; 3365485; -.
DR   KEGG; psb:Psyr_0010; -.
DR   PATRIC; fig|205918.7.peg.10; -.
DR   eggNOG; ENOG4108ZI0; Bacteria.
DR   eggNOG; COG0241; LUCA.
DR   HOGENOM; HOG000016503; -.
DR   KO; K03273; -.
DR   OMA; EHQICLE; -.
DR   BioCyc; PSYR205918:G1G4J-10-MONOMER; -.
DR   Proteomes; UP000000426; 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; TIGR01662; HAD-SF-IIIA; 1.
DR   TIGRFAMs; TIGR01656; Histidinol-ppas; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q500T8.
DR   SWISS-2DPAGE; Q500T8.
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR004682};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR004682,
KW   ECO:0000256|SAAS:SAAS00455224};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR004682,
KW   ECO:0000256|SAAS:SAAS00455242, ECO:0000313|EMBL:AAY35084.1};
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   ACT_SITE      7      7       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR004682-1}.
FT   ACT_SITE      9      9       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR004682-1}.
FT   METAL         7      7       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR004682-4}.
FT   METAL         9      9       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR004682-4}.
FT   METAL        89     89       Zinc. {ECO:0000256|PIRSR:PIRSR004682-4}.
FT   METAL        91     91       Zinc; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR004682-4}.
FT   METAL        97     97       Zinc. {ECO:0000256|PIRSR:PIRSR004682-4}.
FT   METAL        99     99       Zinc. {ECO:0000256|PIRSR:PIRSR004682-4}.
FT   METAL       126    126       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR004682-4}.
FT   SITE         50     50       Stabilizes the phosphoryl group.
FT                                {ECO:0000256|PIRSR:PIRSR004682-3}.
FT   SITE        100    100       Contributes to substrate recognition.
FT                                {ECO:0000256|PIRSR:PIRSR004682-3}.
FT   SITE        101    101       Stabilizes the phosphoryl group.
FT                                {ECO:0000256|PIRSR:PIRSR004682-3}.
SQ   SEQUENCE   180 AA;  19146 MW;  E88D38DD9D26373C CRC64;
     MKLLILDRDG VINHDSDTYI KSVAEWLPIP GSIEAIAALS KAGWTVAVAT NQSGIARGYY
     DLATLDAMHV RLRKLVAEQG GELGLIVYCP HGPDDGCTCR KPKPGMLRAI ARHYAADLKG
     LWFVGDSKGD LQAALAVDSQ PVLVMTGKGR KTMEGGVPAG TLIFDDLAAV AAELIHNSTH
//

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