(data stored in ACNUC9543 zone)

SWISSPROT: A0A0E1NR66_YERPA

ID   A0A0E1NR66_YERPA        Unreviewed;       188 AA.
AC   A0A0E1NR66;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-MAY-2019, entry version 24.
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=YPA_0551 {ECO:0000313|EMBL:ABG12519.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12519.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12519.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12519.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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; CP000308; ABG12519.1; -; Genomic_DNA.
DR   RefSeq; WP_002220062.1; NZ_CP009906.1.
DR   SMR; A0A0E1NR66; -.
DR   EnsemblBacteria; ABG12519; ABG12519; YPA_0551.
DR   EnsemblBacteria; AJJ77763; AJJ77763; CH58_3403.
DR   KEGG; ypa:YPA_0551; -.
DR   PATRIC; fig|360102.15.peg.3572; -.
DR   KO; K03273; -.
DR   OMA; EHQICLE; -.
DR   Proteomes; UP000001971; 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; A0A0E1NR66.
DR   SWISS-2DPAGE; A0A0E1NR66.
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR004682};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
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:ABG12519.1};
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   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   188 AA;  20702 MW;  89A3DF0782DED3BA CRC64;
     MTQSVPAIFL DRDGTVNVDH GYVHEIDNFQ FIDGVIDACR ELKEMGFALV LVTNQSGIAR
     GMFTEEQFLS LTEWMDWSLA DRGVDLDGIY FCPHHPDGSV AEFSETCECR KPLPGMLLQA
     QNELNIDMAA SYMVGDKIED MQAALAANIG TKVLVRTGKP VTAEGEAAAD WVLNSLADLP
     KAIKARYK
//

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