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Reviewed, UniProtKB/Swiss-Prot Q8VD52 (PLPP_RAT)

Last modified February 10, 2009. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Pyridoxal phosphate phosphatase
      Short name=PLP phosphatase
    EC=3.1.3.74
Alternative name(s):
    Reg I-binding protein 1
Gene names
Name: Pdxp
Synonyms: Plp, Plpp, Rbp1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and Pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP By similarity.

Catalytic activity

Pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate.

Cofactor

Divalent ions. Magnesium is the most effective By similarity.

Subunit structure

Homodimer By similarity. Interacts with REG1.

Sequence similarities

Belongs to the HAD-like hydrolase superfamily.

Ontologies

Keywords
   LigandMagnesium
Metal-binding
Pyridoxal phosphate
   Molecular functionHydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

pyridoxal phosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Pyridoxal phosphate phosphatase
PRO_0000068839

Sites

Active site251Nucleophile By similarity
Active site271Proton donor By similarity
Metal binding251Magnesium By similarity
Metal binding271Magnesium By similarity
Metal binding2341Magnesium By similarity

Experimental info

Sequence conflict106 – 1083APG → GTR Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8VD52-1 [UniParc].

Last modified January 10, 2006. Version 2.
Checksum: E609DAA5250151C4

FASTA30933,115
        10         20         30         40         50         60 
MARCERLRGA ALRDVLGQAQ GVLFDCDGVL WNGERIVPGA PELLQRLAQA GKATLFVSNN 

        70         80         90        100        110        120 
SRRARPELAL RFARLGFTGL RAEELFSSAV CAARLLRQRL PGPPDAPGAV FVLGGEGLRA 

       130        140        150        160        170        180 
ELRAAGLRLA GDPGDDPRVR AVLVGYDEHF SFAKLTEACA HLRDPDCLLV ATDRDPWHPL 

       190        200        210        220        230        240 
TDGSRTPGTG SLAAAVETAS GRQALVVGKP SPYMFQCITE DFSVDPARML MVGDRLETDI 

       250        260        270        280        290        300 
LFGHRCGMTT VLTLTGVSSL EEAQAYLAAG QHDLVPHYYV ESIADLMEGL GGLSPPPQFP 


DPVDGGYRP 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed: 15057822] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"Isolation of cDNA clone from rat pancreas cDNA library by two hybrid system, clone 13."
Wu H., Zenilman M.E.
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 106-309.
Strain: Wistar.
Tissue: Pancreas.
[3]Lubec G., Chen W.-Q.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 129-138; 141-154; 186-202 AND 236-245, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.

Cross-references

Sequence databases

AABR03056024 Genomic DNA. No translation available.
AF318578 mRNA. Translation: AAL37168.1.
IPIIPI00361415.
UniGeneRn.9374

3D structure databases

SMRQ8VD52. Positions 2-290.
ModBaseSearch...

Genome annotation databases

EnsemblENSRNOG00000009570. Rattus norvegicus. [Contig view]

Organism-specific databases

RGD1586212. Pdxp.

Phylogenomic databases

HOVERGENQ8VD52.

Enzyme and pathway databases

BRENDA3.1.3.74. 248.

Gene expression databases

ArrayExpressQ8VD52.
GermOnlineENSRNOG00000009570. Rattus norvegicus.

Family and domain databases

InterProIPR005834. Dehalogen-like_hydro.
IPR006357. HAD-SF_hydro_IIA.
IPR006349. PGP_euk.
[Graphical view]
PfamPF00702. Hydrolase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01460. HAD-SF-IIA. 1 hit.
TIGR01452. PGP_euk. 1 hit.
ProtoNetSearch...

Entry information

Entry namePLPP_RAT
AccessionPrimary (citable) accession number: Q8VD52
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: January 10, 2006
Last modified: February 10, 2009
This is version 49 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents