GenomeNet

Database: UniProt
Entry: Q9CA90
LinkDB: Q9CA90
Original site: Q9CA90 
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   16-JAN-2019, entry version 126.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RT   glycerate 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
RT   for the same end.";
RL   Plant Physiol. 155:694-705(2011).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate
CC       and hydroxypyruvate (HP) into glycolate and glycerate in the
CC       cytoplasm, thus providing a cytosolic bypass to the
CC       photorespiratory core cycle. Mostly active in the presence of
CC       NADPH and hydroxypyruvate. {ECO:0000269|PubMed:18952776,
CC       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;
CC         EC=1.1.1.79; 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;
CC         EC=1.1.1.81; Evidence={ECO:0000269|PubMed:18952776};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-glycerate + NADP(+) = 3-hydroxypyruvate + H(+) +
CC         NADPH; Xref=Rhea:RHEA:18657, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16659, ChEBI:CHEBI:17180, ChEBI:CHEBI:57783,
CC         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         Note=Derived from EST data. No experimental confirmation
CC         available.;
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}.
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   UniGene; At.27554; -.
DR   ProteinModelPortal; Q9CA90; -.
DR   SMR; Q9CA90; -.
DR   STRING; 3702.AT1G79870.1; -.
DR   iPTMnet; Q9CA90; -.
DR   PaxDb; Q9CA90; -.
DR   PRIDE; Q9CA90; -.
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   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136700; -.
DR   InParanoid; Q9CA90; -.
DR   KO; K15919; -.
DR   OMA; KWIAHNG; -.
DR   OrthoDB; 1378766at2759; -.
DR   PhylomeDB; Q9CA90; -.
DR   BioCyc; ARA:AT1G79870-MONOMER; -.
DR   BioCyc; MetaCyc:AT1G79870-MONOMER; -.
DR   BRENDA; 1.1.1.81; 399.
DR   Reactome; R-ATH-389661; Glyoxylate metabolism and glycine degradation.
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:0005829; C:cytosol; IDA:TAIR.
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: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; Complete proteome; Cytoplasm; Glycolate pathway;
KW   NAD; NADP; Oxidoreductase; Photorespiration; Pyruvate;
KW   Reference proteome.
FT   CHAIN         1    313       Glyoxylate/hydroxypyruvate reductase A
FT                                HPR2.
FT                                /FTId=PRO_0000419952.
FT   NP_BIND     152    155       NADP. {ECO:0000250}.
FT   NP_BIND     174    176       NADP. {ECO:0000250}.
FT   NP_BIND     230    232       NADP. {ECO:0000250}.
FT   NP_BIND     279    281       NADP. {ECO:0000250}.
FT   ACT_SITE    232    232       {ECO:0000250}.
FT   ACT_SITE    261    261       {ECO:0000250}.
FT   ACT_SITE    279    279       Proton donor. {ECO:0000250}.
FT   BINDING     256    256       NADP. {ECO:0000250}.
FT   VAR_SEQ     134    152       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=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
//
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