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Q9FIZ7

- OPLA_ARATH

UniProt

Q9FIZ7 - OPLA_ARATH

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Protein

5-oxoprolinase

Gene
OXP1, At5g37830, K22F20.70
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Catalyzes the cleavage of 5-oxo-L-proline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate. Acts in the glutathione degradation pathway.1 Publication

Catalytic activityi

ATP + 5-oxo-L-proline + 2 H2O = ADP + phosphate + L-glutamate.

GO - Molecular functioni

  1. 5-oxoprolinase (ATP-hydrolyzing) activity Source: TAIR
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. glutathione catabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT5G37830-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
5-oxoprolinase (EC:3.5.2.9)
Alternative name(s):
5-oxo-L-prolinase
Short name:
5-OPase
Protein OXOPROLINASE 1
Pyroglutamase
Gene namesi
Name:OXP1
Ordered Locus Names:At5g37830
ORF Names:K22F20.70
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G37830.

Subcellular locationi

Cytoplasm Inferred

GO - Cellular componenti

  1. cytoplasm Source: TAIR
  2. cytosol Source: TAIR
  3. plasmodesma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

No morphological phenotype, but high accumulation of 5-oxoproline and decreased concentration of glutamate.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 126612665-oxoprolinasePRO_0000380674Add
BLAST

Proteomic databases

PaxDbiQ9FIZ7.
PRIDEiQ9FIZ7.

Expressioni

Tissue specificityi

Expressed in roots, stems, leaves, flowers and siliques.

Gene expression databases

GenevestigatoriQ9FIZ7.

Interactioni

Protein-protein interaction databases

BioGridi19012. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9FIZ7.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi148 – 1525Poly-Asp
Compositional biasi1258 – 12636Poly-Gly

Sequence similaritiesi

Belongs to the oxoprolinase family.

Phylogenomic databases

eggNOGiCOG0146.
HOGENOMiHOG000047200.
InParanoidiQ9FIZ7.
KOiK01469.
OMAiVEAYMGH.
PhylomeDBiQ9FIZ7.

Family and domain databases

InterProiIPR008040. Hydant_A_N.
IPR002821. Hydantoinase_A.
IPR003692. Hydantoinase_B.
[Graphical view]
PfamiPF05378. Hydant_A_N. 1 hit.
PF01968. Hydantoinase_A. 1 hit.
PF02538. Hydantoinase_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9FIZ7-1 [UniParc]FASTAAdd to Basket

« Hide

MGTVIEGKLR FCIDRGGTFT DVYAEIPGHS DGHVLKLLSV DPSNYDDAPV     50
EGIRRILEEY TGKKIPRTSK IPTDKIQWIR MGTTVATNAL LERKGERIAL 100
CVTKGFKDLL QIGNQARPDI FDLTVAKPSN LYEEVIEVDE RVVLALEDDD 150
DDEGSLIKGV SGEFLRVVKP FDGEGLKPLL KGLLDKGISC LAVVLMHSYT 200
YPKHEMDVEK LALEMGFRHV SLSSALTPMV RAVPRGLTAT VDAYLTPVIK 250
EYLSGFISKF DDDLGKVNVL FMQSDGGLAP ESRFSGHKAV LSGPAGGVVG 300
YSQTLFGLET EKPLIGFDMG GTSTDVSRYD GSYEQVIETQ IAGTIIQAPQ 350
LDINTVAAGG GSKLKFQFGA FRVGPDSVGA HPGPVCYRKG GELAVTDANL 400
VLGFVIPDYF PSIFGPNEDQ PLDVAATREA FEKLAGQINI YRKSQDPSAK 450
DMSVEEIAMG FVSVANETMC RPIRQLTEMK GHETKNHALA CFGGAGPQHA 500
CAIARSLGMK EVLVHRYCGI LSAYGMGLAD VIEDAQEPYS AVYGPESLSE 550
VFRRETVLLR EVREKLQEQG FGDGNISTET YLNLRYDGTD TAIMVKGKKT 600
GDGSAFDYAA EFLKLFEQEY GFKLQNRNLL ICDVRVRGIG VTSILKPRAV 650
EAAPVTPKVE RHYKVYFEGG WHDTPLFKLE NLGFGHEILG PAIIMNGNST 700
VIVEPQCKAI ITKYGNIKIE VEPATSSVKL AENVADVVQL SIFNHRFMGI 750
AEQMGRTLQR TSISTNIKER LDFSCALFSP DGGLVANAPH VPVHLGAMSS 800
TVRWQLKHWG ENLNEGDVLV TNHPCAGGSH LPDITVITPV FDKGKLVFFV 850
ASRGHHAEVG GITPGSMPPF SKAIWEEGAA IKAFKVVEKG VFQEEGIVKL 900
LQFPSSDETT TKIPGTRRIQ DNLSDLQAQI AANQRGISLI KELIEQYGLG 950
TVQAYMKYVQ LNAEEAVREM LKSVANRVSS ETPNSRVGNS VTIEEEDYMD 1000
DGSIIHLKLT IDADKGEASF DFTGTSPEVY GNWNAPEAVT SAAVIYCLRC 1050
LVNVDIPLNQ GCLAPVEIRI PAGSFLSPSE KAAVVGGNVL TSQRVTDVVL 1100
TAFQACACSQ GCMNNLTFGD DTFGYYETIG GGCGAGPTWN GTSGVQCHMT 1150
NTRMTDPEIF EQRYPVLLHR FGLRENSGGN GLHKGGDGLV REIEFRKPVV 1200
VSILSERRVH SPRGLNGGQN GLRGANYLIT KDKRRIYLGG KNTVHVEAGE 1250
ILQILTPGGG GFGSNI 1266
Length:1,266
Mass (Da):137,531
Last modified:March 1, 2001 - v1
Checksum:i77E862B3E4EB7395
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB016873 Genomic DNA. Translation: BAB10362.1.
CP002688 Genomic DNA. Translation: AED94237.1.
AY102096 mRNA. Translation: AAM26666.1.
BT004510 mRNA. Translation: AAO42756.1.
AK228904 mRNA. Translation: BAF00793.1.
RefSeqiNP_198599.1. NM_123142.4.
UniGeneiAt.30461.

Genome annotation databases

EnsemblPlantsiAT5G37830.1; AT5G37830.1; AT5G37830.
GeneIDi833761.
KEGGiath:AT5G37830.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB016873 Genomic DNA. Translation: BAB10362.1 .
CP002688 Genomic DNA. Translation: AED94237.1 .
AY102096 mRNA. Translation: AAM26666.1 .
BT004510 mRNA. Translation: AAO42756.1 .
AK228904 mRNA. Translation: BAF00793.1 .
RefSeqi NP_198599.1. NM_123142.4.
UniGenei At.30461.

3D structure databases

ProteinModelPortali Q9FIZ7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 19012. 1 interaction.

Proteomic databases

PaxDbi Q9FIZ7.
PRIDEi Q9FIZ7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G37830.1 ; AT5G37830.1 ; AT5G37830 .
GeneIDi 833761.
KEGGi ath:AT5G37830.

Organism-specific databases

TAIRi AT5G37830.

Phylogenomic databases

eggNOGi COG0146.
HOGENOMi HOG000047200.
InParanoidi Q9FIZ7.
KOi K01469.
OMAi VEAYMGH.
PhylomeDBi Q9FIZ7.

Enzyme and pathway databases

BioCyci ARA:AT5G37830-MONOMER.

Miscellaneous databases

PROi Q9FIZ7.

Gene expression databases

Genevestigatori Q9FIZ7.

Family and domain databases

InterProi IPR008040. Hydant_A_N.
IPR002821. Hydantoinase_A.
IPR003692. Hydantoinase_B.
[Graphical view ]
Pfami PF05378. Hydant_A_N. 1 hit.
PF01968. Hydantoinase_A. 1 hit.
PF02538. Hydantoinase_B. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence features of the regions of 1,013,767 bp covered by sixteen physically assigned P1 and TAC clones."
    Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N., Tabata S.
    DNA Res. 5:297-308(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-963.
    Strain: cv. Columbia.
  5. "A gamma-glutamyl transpeptidase-independent pathway of glutathione catabolism to glutamate via 5-oxoproline in Arabidopsis."
    Ohkama-Ohtsu N., Oikawa A., Zhao P., Xiang C., Saito K., Oliver D.J.
    Plant Physiol. 148:1603-1613(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiOPLA_ARATH
AccessioniPrimary (citable) accession number: Q9FIZ7
Secondary accession number(s): Q0WQ06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 1, 2001
Last modified: May 14, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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