(data stored in SCRATCH zone)

SWISSPROT: Q145K4_PARXL

ID   Q145K4_PARXL            Unreviewed;       184 AA.
AC   Q145K4;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   RecName: Full=D,D-heptose 1,7-bisphosphate phosphatase {ECO:0000256|PIRNR:PIRNR004682};
DE            EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR004682};
GN   ORFNames=Bxe_A4014 {ECO:0000313|EMBL:ABE28985.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28985.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28985.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28985.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(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; CP000270; ABE28985.1; -; Genomic_DNA.
DR   RefSeq; WP_011486810.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A4014; -.
DR   EnsemblBacteria; ABE28985; ABE28985; Bxe_A4014.
DR   GeneID; 4003393; -.
DR   KEGG; bxb:DR64_1691; -.
DR   KEGG; bxe:Bxe_A4014; -.
DR   PATRIC; fig|266265.5.peg.472; -.
DR   eggNOG; ENOG4108ZI0; Bacteria.
DR   eggNOG; COG0241; LUCA.
DR   HOGENOM; HOG000016503; -.
DR   KO; K03273; -.
DR   OMA; EHQICLE; -.
DR   OrthoDB; 1472357at2; -.
DR   BioCyc; BXEN266265:BXE_RS02240-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 1.
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; Q145K4.
DR   SWISS-2DPAGE; Q145K4.
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR004682};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
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:ABE28985.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR004682-4};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR004682-4,
KW   ECO:0000256|SAAS:SAAS00863697};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Zinc {ECO:0000256|PIRSR:PIRSR004682-4}.
FT   ACT_SITE     10     10       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR004682-1}.
FT   ACT_SITE     12     12       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR004682-1}.
FT   METAL        10     10       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR004682-4}.
FT   METAL        12     12       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       100    100       Zinc. {ECO:0000256|PIRSR:PIRSR004682-4}.
FT   METAL       102    102       Zinc. {ECO:0000256|PIRSR:PIRSR004682-4}.
FT   METAL       129    129       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR004682-4}.
FT   SITE         53     53       Stabilizes the phosphoryl group.
FT                                {ECO:0000256|PIRSR:PIRSR004682-3}.
FT   SITE        103    103       Contributes to substrate recognition.
FT                                {ECO:0000256|PIRSR:PIRSR004682-3}.
FT   SITE        104    104       Stabilizes the phosphoryl group.
FT                                {ECO:0000256|PIRSR:PIRSR004682-3}.
SQ   SEQUENCE   184 AA;  19792 MW;  06C8A0F5590427AE CRC64;
     MPTKKVVILD RDGVINVDSD AFIKSPDEWV ALPGALEAIA RLNQAGYRVA IATNQSGIGR
     GLFDMNALNA MHLKMHRMAA AVGGRIDAVF FCPHTAEDHC ECRKPKPGML KMITERFEVD
     PENTPVVGDA MRDLQAGAAL GHPVHLVLTG KGRKTLAAGG LPEGTIVHDD LRAFALDFLA
     DAQE
//

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