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0PLPP_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePDXP
DescriptionPyridoxal phosphate phosphatase (ec 3.1.3.74) (plp phosphatase).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This group of hydrolase enzymes is structurally different from the alpha/beta hydrolase family (abhydrolase). This group includes L-2-haloacid dehalogenase.poxide hydrolases and phosphatases. The structure consists of two domains. One is an inserted four helix bundle.hich is the least well conserved region of the alignment.etween residues 16 and 96 of HAD1_PSESP. The rest of the fold is composed of the core alpha/beta domain.
  IPR005834:Haloacid dehalogenase-like hydrolase
This family of sequences represent 2-phosphoglycolate phosphatase which is limited to the eukaryotic lineage. PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In mammals.GP is found in many tissues.otably in red blood cells where P-glycolate is and important activator of the hydrolysis of 2.-bisphosphoglycerate. major modifier of the oxygen affinity of hemoglobin. The PGPase enzyme described here is a member of the Haloacid dehalogenase superfamily of hydrolase enzymes. Unlike the bacterial PGP equivalog ().hich is a member of class (subfamily) I.his enzyme is a member of class (subfamily) II . These two enzymes have almost certainly arisen from convergent evolution (although these two ancestors may themselves have diverged from a more distant HAD superfamily progenitor). One of the sequences in the group comes from Chlamydomonas reinhardtii. photosynthetic alga. The enzyme has been purified and characterized and these data are fully consistent with the assignment of function as a PGPase involved in photorespiration . Another.rom Homo sapiens.s supported as a member of the family indirectly. Biochemical characterization of partially purified PGPs from various tissues including red blood cells have been performed while one gene for PGP has been localized to chromosome 16p13.3 . The Homo sapiens sequence maps to chromosome 22. There is indeed a related gene on chromosome 16 (and it is expressed.ince ESTs are found) which shows 46% identity and 59% positives by BLAST2 (E=1e-66). Presumably.hese two genes are isoforms and have the same catalytic function while being expressed in different tissues and may be differently regulated. The sequence from Caenorhabditis elegans.s only supported by sequence similarity. This family is closely related to a family of bacterial sequences including the Escherichia coli NagD and Bacillus subtilus AraL genes which are characterized by the ability to hydrolyze para-nitrophenylphosphate (pNPPases or NPPases). The Chlamydomonas reinhardtii PGPase does not catalyze this reaction and so presumably these two groups have different functions and substrate specificities. Many of the genes in this family have been annotated as pNPPases due to this association.
  IPR006349:2-phosphoglycolate phosphatase, eukaryotic
These sequences form one of the structural subclasss of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs . The classes are defined based on the location and the observed or predicted fold of a so-called "capping domain" .r the absence of such a domain. Class I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Class II consists of sequences in which the capping domain is found between the second and third motifs. Class III sequences have no capping domain in either of these positions. The Class IIA capping domain is predicted to consist of a mixed alpha-beta fold with the basic pattern: Helix-Helix-Helix-Sheet-Helix-Loop-Sheet-Helix-Sheet-Helix. Presently.his subfamily covers the eukaryotic phosphoglycolate phosphatase.s well as four further subfamilies covering closely related sequences in eukaryotes.n Gram-positive bacteria and in Gram-negative bacteria. The Escherishia coli NagD gene and the Bacillus subtilus AraL gene are members of this subfamily but are not members of the any of the presently defined equivalogs within it. NagD is part of the NAG operon responsible for N-acetylglucosamine metabolism . The function of this gene is unknown. Genes from several organisms have been annotated as NagD.r NagD-like. However.ithout data on the presence of other members of this pathway.such as in the case of Yersinia pestis) these assignments should not be given great weight. The AraL gene is similar.t is part of the L-arabinose operon.ut the function is unknown . A gene from Halobacterium has been annotated as AraL.ut no other Ara operon genes have been annotated. Many of the genes in this subfamily have been annotated as "pNPPase" "4-nitrophenyl phosphatase" or "NPPase". These all refer to the same activity versus a common lab test compound used to determine phosphatase activity. There is no evidence that this activity is physiologically relevant.
  IPR006357:HAD-superfamily hydrolase, subfamily IIA
IPR005834:Hydrolase 
Evalue:-22.0457572937012 
Location:19-260
SequencesProtein: PLPP_HUMAN (296 aa)
mRNA: NM_020315
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords)
KO assignmentK07758
  Level 3 annotation:
    pyridoxal phosphatase
  Level 2 annotation:
    Other enzymes
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 68 residues, 36365427-36365629Exon2: 50 residues, 36365655-36365799Exon3: 37 residues, 36367326-36367431Exon4: 27 residues, 36368491-36368568Exon5: 39 residues, 36368847-36368959Exon6: 27 residues, 36369050-36369127Exon7: 50 residues, 36369596-36369741Exon8: 25 residues, 36370589-36370658Exon9: 32 residues, 36370822-36370913Exon10: 50 residues, 36371317-36371463Exon11: 39 residues, 36372770-36372882Exon12: 29 residues, 36373219-36373301Exon13: 29 residues, 36373393-36373474Exon14: 41 residues, 36374271-36374388Exon15: 34 residues, 36376104-36376202Exon16: 63 residues, 36376494-36376678Exon17: 33 residues, 36379731-36379826Exon18: 461 residues, 36391507-36392885Exon19: 2 residues, -Jump to Q6ZT62_HUMANExon1: 57 residues, 36365629-36365799Exon2: 16 residues, 36367078-36367121Exon3: 37 residues, 36367326-36367431Exon4: 27 residues, 36368491-36368568Exon5: 39 residues, 36368847-36368959Exon6: 27 residues, 36369050-36369127Exon7: 50 residues, 36369596-36369741Exon8: 25 residues, 36370589-36370658Exon9: 32 residues, 36370822-36370913Exon10: 50 residues, 36371317-36371463Exon11: 39 residues, 36372770-36372882Exon12: 29 residues, 36373219-36373301Exon13: 29 residues, 36373393-36373474Exon14: 41 residues, 36374271-36374388Exon15: 34 residues, 36376104-36376202Exon16: 63 residues, 36376494-36376678Exon17: 33 residues, 36379731-36379826Exon18: 259 residues, 36381224-36381995Exon19: 2 residues, -Jump to 3BP1_HUMANExon1: 210 residues, 36384682-36385309Exon2: 461 residues, 36391507-36392885Exon3: 2 residues, -Jump to PLPP_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3313 36334448-36359516 ~-25K 24689(GGA1)(+)Loci: 3314 36365427-36392885 ~-27K 24693(+)Loci: 3315 36533890-36543129 ~-9K 24705(GCAT)(+)Loci: 3316 36549334-36551448 ~-2K 24707(GALR3)(+)Loci: 3317 36783348-36801653 ~-18K 24722(PRKCABP)(+)Loci: 4568 36810855-36836622 ~-26K 24725(-)Loci: 4569 37152280-37181149 ~-29K 24733(KCNJ4)(-)Loci: 4570 37209390-37232262 ~-23K 24737(DDX17)(-)Loci: 4571 37460680-37481928 ~-21K 24750(UNC84B)(-)Loci: 4567 35932191-35938299 ~-6K 24676(SSTR3)(-)Link out to UCSC