GenomeNet

Database: UniProt
Entry: Q9C9W5
LinkDB: Q9C9W5
Original site: Q9C9W5 
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   16-JAN-2019, entry version 135.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
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   [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
RT   reference 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.,
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   [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.,
RA   Hayashizaki Y., 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.,
RA   Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT   "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel
RT   targeting 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.,
RA   Seki M., 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
RT   glycerate during photorespiration in Arabidopsis.";
RL   Plant Cell 20:2848-2859(2008).
RN   [9]
RP   CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION BY DROUGHT AND
RP   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
RT   supported by peroxisomal hydroxypyruvate reductase when malate
RT   dehydrogenase is 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
RT   for 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.,
RA   Badger M.R.;
RT   "Peroxisomal hydroxypyruvate reductase is not essential for
RT   photorespiration in Arabidopsis but its absence causes an increase in
RT   the stoichiometry of photorespiratory CO2 release.";
RL   Photosyn. Res. 108:91-100(2011).
CC   -!- FUNCTION: Catalyzes the NADH-dependent reduction of
CC       hydroxypyruvate into glycerate in the photorespiratory core cycle.
CC       Mediates fatty acid beta-oxidation in germinating seeds when
CC       malate dehydrogenase is absent. {ECO:0000269|PubMed:18952776,
CC       ECO:0000269|PubMed:19812894, ECO:0000269|PubMed:21205613,
CC       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;
CC         EC=1.1.1.29; Evidence={ECO:0000269|PubMed:18952776,
CC         ECO:0000269|PubMed:19529821};
CC   -!- ACTIVITY REGULATION: Slightly inhibited by oxalate.
CC       {ECO:0000269|PubMed:18952776}.
CC   -!- PATHWAY: Photosynthesis; photorespiration; 3-phospho-D-glycerate
CC       from 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         Note=Derived from EST data. No experimental confirmation
CC         available.;
CC   -!- TISSUE SPECIFICITY: Present in leaves (at protein level). Mostly
CC       expressed in photosynthetic tissues such as leaves, stems,
CC       flowers, 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,
CC       but transiently repressed in darkness.
CC       {ECO:0000269|PubMed:19529821}.
CC   -!- DISRUPTION PHENOTYPE: Very low NADH-dependent hydroxypyruvate
CC       reductase activity in leaves. Under short days, slower growth and
CC       delayed bolting. Slight accumulation of metabolites with long
CC       turnover half-times that become dissimilated during the dark.
CC       Perturbated photorespiration-related gas exchange. When associated
CC       with HPR2 disruption, strong air-sensitivity and dramatic
CC       reduction in photosynthetic performance.
CC       {ECO:0000269|PubMed:18952776, ECO:0000269|PubMed:21567290}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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   UniGene; At.339; -.
DR   ProteinModelPortal; Q9C9W5; -.
DR   SMR; Q9C9W5; -.
DR   BioGrid; 28350; 3.
DR   IntAct; Q9C9W5; 2.
DR   STRING; 3702.AT1G68010.2; -.
DR   iPTMnet; Q9C9W5; -.
DR   PaxDb; Q9C9W5; -.
DR   PRIDE; Q9C9W5; -.
DR   ProMEX; Q9C9W5; -.
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   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136700; -.
DR   InParanoid; Q9C9W5; -.
DR   KO; K15893; -.
DR   OrthoDB; 1378766at2759; -.
DR   PhylomeDB; Q9C9W5; -.
DR   BioCyc; ARA:AT1G68010-MONOMER; -.
DR   BioCyc; MetaCyc:AT1G68010-MONOMER; -.
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; IDA:TAIR.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   GO; GO:0008266; F:poly(U) RNA binding; IDA:TAIR.
DR   GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
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; Complete proteome; Glycolate pathway; NAD;
KW   Oxidoreductase; Peroxisome; Photorespiration; Pyruvate;
KW   Reference proteome.
FT   CHAIN         1    386       Glycerate dehydrogenase HPR, peroxisomal.
FT                                /FTId=PRO_0000419951.
FT   NP_BIND     175    176       NAD. {ECO:0000250}.
FT   NP_BIND     271    273       NAD. {ECO:0000250}.
FT   NP_BIND     320    323       NAD. {ECO:0000250}.
FT   MOTIF       384    386       Microbody targeting signal.
FT                                {ECO:0000255}.
FT   ACT_SITE    273    273       {ECO:0000250}.
FT   ACT_SITE    302    302       {ECO:0000250}.
FT   ACT_SITE    320    320       Proton donor. {ECO:0000250}.
FT   BINDING     297    297       NAD. {ECO:0000250}.
FT   VAR_SEQ     264    264       K -> KV (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_044376.
FT   CONFLICT    278    278       D -> H (in Ref. 1; BAA19751).
FT                                {ECO:0000305}.
FT   CONFLICT    312    312       T -> M (in Ref. 1; BAA19751).
FT                                {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
//
DBGET integrated database retrieval system