HPR2_ARATH
ID HPR2_ARATH Reviewed; 313 AA.
AC Q9CA90; F4HQC5;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Glyoxylate/hydroxypyruvate reductase A HPR2;
DE EC=1.1.1.79;
DE EC=1.1.1.81;
DE AltName: Full=NAD(P)H-dependent hydroxypyruvate reductase 2;
DE Short=AtHPR2;
DE Short=HPR 2;
GN Name=HPR2; OrderedLocusNames=At1g79870; ORFNames=F19K16.17;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, IDENTIFICATION BY MASS SPECTROMETRY,
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX PubMed=18952776; DOI=10.1105/tpc.108.062265;
RA Timm S., Nunes-Nesi A., Paernik T., Morgenthal K., Wienkoop S.,
RA Keerberg O., Weckwerth W., Kleczkowski L.A., Fernie A.R., Bauwe H.;
RT "A cytosolic pathway for the conversion of hydroxypyruvate to glycerate
RT during photorespiration in Arabidopsis.";
RL Plant Cell 20:2848-2859(2008).
RN [6]
RP FUNCTION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=21205613; DOI=10.1104/pp.110.166538;
RA Timm S., Florian A., Jahnke K., Nunes-Nesi A., Fernie A.R., Bauwe H.;
RT "The hydroxypyruvate-reducing system in Arabidopsis: multiple enzymes for
RT the same end.";
RL Plant Physiol. 155:694-705(2011).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate and
CC hydroxypyruvate (HP) into glycolate and glycerate in the cytoplasm,
CC thus providing a cytosolic bypass to the photorespiratory core cycle.
CC Mostly active in the presence of NADPH and hydroxypyruvate.
CC {ECO:0000269|PubMed:18952776, ECO:0000269|PubMed:21205613}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycolate + NADP(+) = glyoxylate + H(+) + NADPH;
CC Xref=Rhea:RHEA:10992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805,
CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.79;
CC Evidence={ECO:0000269|PubMed:18952776};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + NAD(+) = 3-hydroxypyruvate + H(+) + NADH;
CC Xref=Rhea:RHEA:17905, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:17180, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.81;
CC Evidence={ECO:0000269|PubMed:18952776};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + NADP(+) = 3-hydroxypyruvate + H(+) + NADPH;
CC Xref=Rhea:RHEA:18657, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:17180, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.81;
CC Evidence={ECO:0000269|PubMed:18952776};
CC -!- ACTIVITY REGULATION: Strongly inhibited by oxalate.
CC {ECO:0000269|PubMed:18952776}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18952776}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CA90-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CA90-2; Sequence=VSP_044377;
CC -!- DISRUPTION PHENOTYPE: Elevated levels of hydroxypyruvate and other
CC metabolites in leaves. Under long-day conditions, slightly altered
CC photosynthetic gas exchange. When associated with HPR1 disruption,
CC strong air-sensitivity and dramatic reduction in photosynthetic
CC performance. {ECO:0000269|PubMed:18952776}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. GyaR subfamily. {ECO:0000305}.
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DR EMBL; AC011717; AAG52259.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36315.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36316.1; -; Genomic_DNA.
DR EMBL; AY069901; AAL47452.1; -; mRNA.
DR EMBL; AY113022; AAM47330.1; -; mRNA.
DR EMBL; AY088166; AAM65710.1; -; mRNA.
DR PIR; G96829; G96829.
DR RefSeq; NP_001185444.1; NM_001198515.1. [Q9CA90-2]
DR RefSeq; NP_178105.1; NM_106636.3. [Q9CA90-1]
DR AlphaFoldDB; Q9CA90; -.
DR SMR; Q9CA90; -.
DR BioGRID; 29544; 6.
DR STRING; 3702.AT1G79870.1; -.
DR iPTMnet; Q9CA90; -.
DR PaxDb; Q9CA90; -.
DR PRIDE; Q9CA90; -.
DR ProteomicsDB; 232173; -. [Q9CA90-1]
DR EnsemblPlants; AT1G79870.1; AT1G79870.1; AT1G79870. [Q9CA90-1]
DR EnsemblPlants; AT1G79870.2; AT1G79870.2; AT1G79870. [Q9CA90-2]
DR GeneID; 844326; -.
DR Gramene; AT1G79870.1; AT1G79870.1; AT1G79870. [Q9CA90-1]
DR Gramene; AT1G79870.2; AT1G79870.2; AT1G79870. [Q9CA90-2]
DR KEGG; ath:AT1G79870; -.
DR Araport; AT1G79870; -.
DR TAIR; locus:2017824; AT1G79870.
DR eggNOG; KOG0069; Eukaryota.
DR HOGENOM; CLU_019796_1_2_1; -.
DR InParanoid; Q9CA90; -.
DR OMA; KMKPNCI; -.
DR PhylomeDB; Q9CA90; -.
DR BioCyc; ARA:AT1G79870-MON; -.
DR BioCyc; MetaCyc:AT1G79870-MON; -.
DR BRENDA; 1.1.1.237; 399.
DR BRENDA; 1.1.1.79; 399.
DR BRENDA; 1.1.1.81; 399.
DR PRO; PR:Q9CA90; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CA90; baseline and differential.
DR Genevisible; Q9CA90; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:RHEA.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0047995; F:hydroxyphenylpyruvate reductase activity; IDA:TAIR.
DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR GO; GO:0009854; P:oxidative photosynthetic carbon pathway; IMP:UniProtKB.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Glycolate pathway; NAD; NADP;
KW Oxidoreductase; Photorespiration; Pyruvate; Reference proteome.
FT CHAIN 1..313
FT /note="Glyoxylate/hydroxypyruvate reductase A HPR2"
FT /id="PRO_0000419952"
FT ACT_SITE 232
FT /evidence="ECO:0000250"
FT ACT_SITE 261
FT /evidence="ECO:0000250"
FT ACT_SITE 279
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 152..155
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 174..176
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 230..232
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 279..281
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT VAR_SEQ 134..152
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044377"
SQ SEQUENCE 313 AA; 34161 MW; A8D52C698A03B183 CRC64;
MESIGVLMMC PMSSYLENEL EKRFNLLRFW TSPEKSVLLE THRNSIRAVV GNASAGADAQ
LISDLPNLEI VSSFSVGLDK IDLGKCKEKG IRVTNTPDVL TEDVADLAIG LILALLRRLC
ECDRYVRSGK WKQGEFQLTT KFSGKSVGII GLGRIGTAIA KRAEAFSCPI NYYSRTIKPD
VAYKYYPTVV DLAQNSDILV VACPLTEQTR HIVDRQVMDA LGAKGVLINI GRGPHVDEQE
LIKALTEGRL GGAALDVFEQ EPHVPEELFG LENVVLLPHV GSGTVETRNA MADLVVGNLE
AHFSGKSLLT PVV
