(data stored in SCRATCH zone)

SWISSPROT: Q3Z5F7_SHISS

ID   Q3Z5F7_SHISS            Unreviewed;       191 AA.
AC   Q3Z5F7;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 94.
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=yaeD {ECO:0000313|EMBL:AAZ87005.1};
GN   OrderedLocusNames=SSON_0214 {ECO:0000313|EMBL:AAZ87005.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ87005.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ87005.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ87005.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000038; AAZ87005.1; -; Genomic_DNA.
DR   SMR; Q3Z5F7; -.
DR   EnsemblBacteria; AAZ87005; AAZ87005; SSON_0214.
DR   KEGG; ssn:SSON_0214; -.
DR   HOGENOM; HOG000016501; -.
DR   KO; K03273; -.
DR   OMA; EHQICLE; -.
DR   BioCyc; SSON300269:G1GL2-246-MONOMER; -.
DR   Proteomes; UP000002529; 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; Q3Z5F7.
DR   SWISS-2DPAGE; Q3Z5F7.
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR004682};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002529};
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   191 AA;  21294 MW;  E7814B34A23128FA CRC64;
     MAKSVPAIFL DRDGTINVDH GYVHEIDNFE FIDGVIDAMR ELKKMGFALV VVTNQSGIAR
     GKFTEAQFET LTEWMDWSLA DRDVDLDGIY YCPHHPQGSV EEFRQVCDCR KPHPGMLLSA
     RDYLHIDMAA SYMVGDKLED MQAAVAANVG TKVLVRTGKP ITPEAENAAD WVLNSLADLP
     QAIKKQQKPA Q
//

If you have problems or comments...

PBIL Back to PBIL home page