HPR1_ARATH
ID HPR1_ARATH Reviewed; 386 AA.
AC Q9C9W5; B9DHJ0; F4HVJ9; O04213;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Glycerate dehydrogenase HPR, peroxisomal;
DE Short=GDH;
DE EC=1.1.1.29;
DE AltName: Full=NADH-dependent hydroxypyruvate reductase 1;
DE Short=AtHPR1;
DE Short=HPR 1;
GN Name=HPR; OrderedLocusNames=At1g68010; ORFNames=T23K23.14;
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 [MRNA], SUBCELLULAR LOCATION, MICROBODY TARGETING
RP SIGNAL, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9177031; DOI=10.1093/oxfordjournals.pcp.a029188;
RA Mano S., Hayashi M., Kondo M., Nishimura M.;
RT "Hydroxypyruvate reductase with a carboxy-terminal targeting signal to
RT microbodies is expressed in Arabidopsis.";
RL Plant Cell Physiol. 38:449-455(1997).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-386 (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND ACTIVITY
RP 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 [9]
RP CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION BY DROUGHT AND LIGHT.
RX PubMed=19529821; DOI=10.1093/mp/ssn088;
RA Wang Y., Beaith M., Chalifoux M., Ying J., Uchacz T., Sarvas C.,
RA Griffiths R., Kuzma M., Wan J., Huang Y.;
RT "Shoot-specific down-regulation of protein farnesyltransferase (alpha-
RT subunit) for yield protection against drought in canola.";
RL Mol. Plant 2:191-200(2009).
RN [10]
RP FUNCTION.
RX PubMed=19812894; DOI=10.1007/s11103-009-9554-2;
RA Pracharoenwattana I., Zhou W., Smith S.M.;
RT "Fatty acid beta-oxidation in germinating Arabidopsis seeds is supported by
RT peroxisomal hydroxypyruvate reductase when malate dehydrogenase is
RT absent.";
RL Plant Mol. Biol. 72:101-109(2010).
RN [11]
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).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21567290; DOI=10.1007/s11120-011-9651-3;
RA Cousins A.B., Walker B.J., Pracharoenwattana I., Smith S.M., Badger M.R.;
RT "Peroxisomal hydroxypyruvate reductase is not essential for
RT photorespiration in Arabidopsis but its absence causes an increase in the
RT stoichiometry of photorespiratory CO2 release.";
RL Photosyn. Res. 108:91-100(2011).
CC -!- FUNCTION: Catalyzes the NADH-dependent reduction of hydroxypyruvate
CC into glycerate in the photorespiratory core cycle. Mediates fatty acid
CC beta-oxidation in germinating seeds when malate dehydrogenase is
CC absent. {ECO:0000269|PubMed:18952776, ECO:0000269|PubMed:19812894,
CC ECO:0000269|PubMed:21205613, ECO:0000269|PubMed:21567290}.
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=1.1.1.29;
CC Evidence={ECO:0000269|PubMed:18952776, ECO:0000269|PubMed:19529821};
CC -!- ACTIVITY REGULATION: Slightly inhibited by oxalate.
CC {ECO:0000269|PubMed:18952776}.
CC -!- PATHWAY: Photosynthesis; photorespiration; 3-phospho-D-glycerate from
CC glycine: step 3/4.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:9177031}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C9W5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C9W5-2; Sequence=VSP_044376;
CC -!- TISSUE SPECIFICITY: Present in leaves (at protein level). Mostly
CC expressed in photosynthetic tissues such as leaves, stems, flowers,
CC buds, and, to a lower extent, in siliques and roots.
CC {ECO:0000269|PubMed:19529821, ECO:0000269|PubMed:9177031}.
CC -!- INDUCTION: Induced by drought. Accumulates in response to light, but
CC transiently repressed in darkness. {ECO:0000269|PubMed:19529821}.
CC -!- DISRUPTION PHENOTYPE: Very low NADH-dependent hydroxypyruvate reductase
CC activity in leaves. Under short days, slower growth and delayed
CC bolting. Slight accumulation of metabolites with long turnover half-
CC times that become dissimilated during the dark. Perturbated
CC photorespiration-related gas exchange. When associated with HPR2
CC disruption, strong air-sensitivity and dramatic reduction in
CC photosynthetic performance. {ECO:0000269|PubMed:18952776,
CC ECO:0000269|PubMed:21567290}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; D85339; BAA19751.1; -; mRNA.
DR EMBL; AC012563; AAG52006.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34735.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34736.1; -; Genomic_DNA.
DR EMBL; AF370221; AAK44036.1; -; mRNA.
DR EMBL; AY099552; AAM20404.1; -; mRNA.
DR EMBL; AY113871; AAM44919.1; -; mRNA.
DR EMBL; BT001237; AAN65124.1; -; mRNA.
DR EMBL; AK226564; BAE98694.1; -; mRNA.
DR EMBL; AK317543; BAH20207.1; -; mRNA.
DR PIR; B96703; B96703.
DR RefSeq; NP_001185349.1; NM_001198420.1. [Q9C9W5-2]
DR RefSeq; NP_176968.1; NM_105471.4. [Q9C9W5-1]
DR AlphaFoldDB; Q9C9W5; -.
DR SMR; Q9C9W5; -.
DR BioGRID; 28350; 3.
DR IntAct; Q9C9W5; 2.
DR STRING; 3702.AT1G68010.2; -.
DR iPTMnet; Q9C9W5; -.
DR MetOSite; Q9C9W5; -.
DR PaxDb; Q9C9W5; -.
DR PRIDE; Q9C9W5; -.
DR ProMEX; Q9C9W5; -.
DR ProteomicsDB; 232150; -. [Q9C9W5-1]
DR EnsemblPlants; AT1G68010.1; AT1G68010.1; AT1G68010. [Q9C9W5-1]
DR EnsemblPlants; AT1G68010.2; AT1G68010.2; AT1G68010. [Q9C9W5-2]
DR GeneID; 843129; -.
DR Gramene; AT1G68010.1; AT1G68010.1; AT1G68010. [Q9C9W5-1]
DR Gramene; AT1G68010.2; AT1G68010.2; AT1G68010. [Q9C9W5-2]
DR KEGG; ath:AT1G68010; -.
DR Araport; AT1G68010; -.
DR TAIR; locus:2200231; AT1G68010.
DR eggNOG; KOG0069; Eukaryota.
DR HOGENOM; CLU_019796_1_2_1; -.
DR InParanoid; Q9C9W5; -.
DR OrthoDB; 1378766at2759; -.
DR PhylomeDB; Q9C9W5; -.
DR BioCyc; ARA:AT1G68010-MON; -.
DR BioCyc; MetaCyc:AT1G68010-MON; -.
DR BRENDA; 1.1.1.26; 399.
DR BRENDA; 1.1.1.29; 399.
DR BRENDA; 1.1.1.81; 399.
DR UniPathway; UPA00951; UER00916.
DR PRO; PR:Q9C9W5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9W5; baseline and differential.
DR Genevisible; Q9C9W5; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IBA:GO_Central.
DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:TAIR.
DR GO; GO:0071482; P:cellular response to light stimulus; IEP:UniProtKB.
DR GO; GO:0042631; P:cellular response to water deprivation; IEP:UniProtKB.
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; Glycolate pathway; NAD; Oxidoreductase; Peroxisome;
KW Photorespiration; Pyruvate; Reference proteome.
FT CHAIN 1..386
FT /note="Glycerate dehydrogenase HPR, peroxisomal"
FT /id="PRO_0000419951"
FT MOTIF 384..386
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 273
FT /evidence="ECO:0000250"
FT ACT_SITE 302
FT /evidence="ECO:0000250"
FT ACT_SITE 320
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 175..176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 271..273
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 320..323
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT VAR_SEQ 264
FT /note="K -> KV (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044376"
FT CONFLICT 278
FT /note="D -> H (in Ref. 1; BAA19751)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="T -> M (in Ref. 1; BAA19751)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 386 AA; 42248 MW; CF900B10C44055BD CRC64;
MAKPVSIEVY NPNGKYRVVS TKPMPGTRWI NLLVDQGCRV EICHLKKTIL SVEDIIDLIG
DKCDGVIGQL TEDWGETLFS ALSKAGGKAF SNMAVGYNNV DVEAANKYGI AVGNTPGVLT
ETTAELAASL SLAAARRIVE ADEFMRGGLY EGWLPHLFVG NLLKGQTVGV IGAGRIGSAY
ARMMVEGFKM NLIYFDLYQS TRLEKFVTAY GQFLKANGEQ PVTWKRASSM EEVLREADLI
SLHPVLDKTT YHLVNKERLA MMKKEAILVN CSRGPVIDEA ALVEHLKENP MFRVGLDVFE
EEPFMKPGLA DTKNAIVVPH IASASKWTRE GMATLAALNV LGRVKGYPIW HDPNRVDPFL
NENASPPNAS PSIVNSKALG LPVSKL
