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Protein

Glyoxylate/hydroxypyruvate reductase A HPR2

Gene

HPR2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate (HP) into glycolate and glycerate in the cytoplasm, thus providing a cytosolic bypass to the photorespiratory core cycle. Mostly active in the presence of NADPH and hydroxypyruvate.2 Publications

Catalytic activityi

Glycolate + NADP+ = glyoxylate + NADPH.1 Publication
D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H.1 Publication

Enzyme regulationi

Strongly inhibited by oxalate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei232 – 2321By similarity
Binding sitei256 – 2561NADPBy similarity
Active sitei261 – 2611By similarity
Active sitei279 – 2791Proton donorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi152 – 1554NADPBy similarity
Nucleotide bindingi174 – 1763NADPBy similarity
Nucleotide bindingi230 – 2323NADPBy similarity
Nucleotide bindingi279 – 2813NADPBy similarity

GO - Molecular functioni

  • glyoxylate reductase (NADP) activity Source: UniProtKB
  • hydroxypyruvate reductase activity Source: UniProtKB
  • NAD binding Source: InterPro

GO - Biological processi

  • oxidative photosynthetic carbon pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolate pathway, Photorespiration

Keywords - Ligandi

NAD, NADP, Pyruvate

Enzyme and pathway databases

BioCyciARA:AT1G79870-MONOMER.
ARA:GQT-1734-MONOMER.
BRENDAi1.1.1.81. 399.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyoxylate/hydroxypyruvate reductase A HPR2 (EC:1.1.1.79, EC:1.1.1.81)
Alternative name(s):
NAD(P)H-dependent hydroxypyruvate reductase 2
Short name:
AtHPR2
Short name:
HPR 2
Gene namesi
Name:HPR2
Ordered Locus Names:At1g79870
ORF Names:F19K16.17
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G79870.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Elevated levels of hydroxypyruvate and other metabolites in leaves. Under long-day conditions, slightly altered photosynthetic gas exchange. When associated with HPR1 disruption, strong air-sensitivity and dramatic reduction in photosynthetic performance.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Glyoxylate/hydroxypyruvate reductase A HPR2PRO_0000419952Add
BLAST

Proteomic databases

PaxDbiQ9CA90.
PRIDEiQ9CA90.

PTM databases

iPTMnetiQ9CA90.

Expressioni

Gene expression databases

GenevisibleiQ9CA90. AT.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi3702.AT1G79870.1.

Structurei

3D structure databases

ProteinModelPortaliQ9CA90.
SMRiQ9CA90. Positions 2-313.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0069. Eukaryota.
COG1052. LUCA.
HOGENOMiHOG000136700.
InParanoidiQ9CA90.
KOiK15919.
OMAiQRTKQDH.
PhylomeDBiQ9CA90.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029752. D-isomer_DH_CS1.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9CA90-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MESIGVLMMC PMSSYLENEL EKRFNLLRFW TSPEKSVLLE THRNSIRAVV
60 70 80 90 100
GNASAGADAQ LISDLPNLEI VSSFSVGLDK IDLGKCKEKG IRVTNTPDVL
110 120 130 140 150
TEDVADLAIG LILALLRRLC ECDRYVRSGK WKQGEFQLTT KFSGKSVGII
160 170 180 190 200
GLGRIGTAIA KRAEAFSCPI NYYSRTIKPD VAYKYYPTVV DLAQNSDILV
210 220 230 240 250
VACPLTEQTR HIVDRQVMDA LGAKGVLINI GRGPHVDEQE LIKALTEGRL
260 270 280 290 300
GGAALDVFEQ EPHVPEELFG LENVVLLPHV GSGTVETRNA MADLVVGNLE
310
AHFSGKSLLT PVV
Length:313
Mass (Da):34,161
Last modified:June 1, 2001 - v1
Checksum:iA8D52C698A03B183
GO
Isoform 2 (identifier: Q9CA90-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     134-152: Missing.

Note: Derived from EST data. No experimental confirmation available.
Show »
Length:294
Mass (Da):32,197
Checksum:i55F17371E075DB34
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei134 – 15219Missing in isoform 2. CuratedVSP_044377Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC011717 Genomic DNA. Translation: AAG52259.1.
CP002684 Genomic DNA. Translation: AEE36315.1.
CP002684 Genomic DNA. Translation: AEE36316.1.
AY069901 mRNA. Translation: AAL47452.1.
AY113022 mRNA. Translation: AAM47330.1.
AY088166 mRNA. Translation: AAM65710.1.
PIRiG96829.
RefSeqiNP_001185444.1. NM_001198515.1. [Q9CA90-2]
NP_178105.1. NM_106636.2. [Q9CA90-1]
UniGeneiAt.27554.

Genome annotation databases

EnsemblPlantsiAT1G79870.1; AT1G79870.1; AT1G79870. [Q9CA90-1]
GeneIDi844326.
KEGGiath:AT1G79870.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC011717 Genomic DNA. Translation: AAG52259.1.
CP002684 Genomic DNA. Translation: AEE36315.1.
CP002684 Genomic DNA. Translation: AEE36316.1.
AY069901 mRNA. Translation: AAL47452.1.
AY113022 mRNA. Translation: AAM47330.1.
AY088166 mRNA. Translation: AAM65710.1.
PIRiG96829.
RefSeqiNP_001185444.1. NM_001198515.1. [Q9CA90-2]
NP_178105.1. NM_106636.2. [Q9CA90-1]
UniGeneiAt.27554.

3D structure databases

ProteinModelPortaliQ9CA90.
SMRiQ9CA90. Positions 2-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G79870.1.

PTM databases

iPTMnetiQ9CA90.

Proteomic databases

PaxDbiQ9CA90.
PRIDEiQ9CA90.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G79870.1; AT1G79870.1; AT1G79870. [Q9CA90-1]
GeneIDi844326.
KEGGiath:AT1G79870.

Organism-specific databases

TAIRiAT1G79870.

Phylogenomic databases

eggNOGiKOG0069. Eukaryota.
COG1052. LUCA.
HOGENOMiHOG000136700.
InParanoidiQ9CA90.
KOiK15919.
OMAiQRTKQDH.
PhylomeDBiQ9CA90.

Enzyme and pathway databases

BioCyciARA:AT1G79870-MONOMER.
ARA:GQT-1734-MONOMER.
BRENDAi1.1.1.81. 399.

Miscellaneous databases

PROiQ9CA90.

Gene expression databases

GenevisibleiQ9CA90. AT.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029752. D-isomer_DH_CS1.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [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] (ISOFORM 1).
    Strain: cv. Columbia.
  4. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "A cytosolic pathway for the conversion of hydroxypyruvate to glycerate during photorespiration in Arabidopsis."
    Timm S., Nunes-Nesi A., Paernik T., Morgenthal K., Wienkoop S., Keerberg O., Weckwerth W., Kleczkowski L.A., Fernie A.R., Bauwe H.
    Plant Cell 20:2848-2859(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ENZYME REGULATION.
  6. "The hydroxypyruvate-reducing system in Arabidopsis: multiple enzymes for the same end."
    Timm S., Florian A., Jahnke K., Nunes-Nesi A., Fernie A.R., Bauwe H.
    Plant Physiol. 155:694-705(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: cv. Columbia and cv. Landsberg erecta.

Entry informationi

Entry nameiHPR2_ARATH
AccessioniPrimary (citable) accession number: Q9CA90
Secondary accession number(s): F4HQC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 109 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.