HPR3_ARATH
ID HPR3_ARATH Reviewed; 323 AA.
AC Q9LE33;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Glyoxylate/hydroxypyruvate reductase HPR3;
DE EC=1.1.1.79 {ECO:0000305|PubMed:21205613};
DE EC=1.1.1.81 {ECO:0000305|PubMed:21205613};
DE AltName: Full=NAD(P)H-dependent hydroxypyruvate reductase 3;
DE Short=AtHPR3;
DE Short=HPR 3;
GN Name=HPR3; OrderedLocusNames=At1g12550; ORFNames=F5O11.29, T12C24.9;
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].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND ACTIVITY
RP REGULATION.
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. Mostly active in the
CC presence of NADPH and glyoxylate. {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:0000305|PubMed:21205613};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10994;
CC Evidence={ECO:0000305|PubMed:21205613};
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:0000305|PubMed:21205613};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18659;
CC Evidence={ECO:0000305|PubMed:21205613};
CC -!- ACTIVITY REGULATION: Inhibited by oxalate.
CC {ECO:0000269|PubMed:21205613}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Disrupted photorespiratory flux leading to a
CC slight altered leaf concentrations of the photorespiratory
CC intermediates hydroxypyruvate (HP), glycerate, and glycine.
CC {ECO:0000269|PubMed:21205613}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. GyaR subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC025416; AAF79644.1; -; Genomic_DNA.
DR EMBL; AC025417; AAF88077.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28896.1; -; Genomic_DNA.
DR EMBL; BT011735; AAS49098.1; -; mRNA.
DR EMBL; AK221605; BAD95166.1; -; mRNA.
DR RefSeq; NP_172716.1; NM_101126.3.
DR AlphaFoldDB; Q9LE33; -.
DR SMR; Q9LE33; -.
DR STRING; 3702.AT1G12550.1; -.
DR PaxDb; Q9LE33; -.
DR PRIDE; Q9LE33; -.
DR ProteomicsDB; 230233; -.
DR EnsemblPlants; AT1G12550.1; AT1G12550.1; AT1G12550.
DR GeneID; 837811; -.
DR Gramene; AT1G12550.1; AT1G12550.1; AT1G12550.
DR KEGG; ath:AT1G12550; -.
DR Araport; AT1G12550; -.
DR TAIR; locus:2034665; AT1G12550.
DR eggNOG; KOG0069; Eukaryota.
DR HOGENOM; CLU_019796_1_2_1; -.
DR InParanoid; Q9LE33; -.
DR OMA; KVISCHS; -.
DR OrthoDB; 1378766at2759; -.
DR PhylomeDB; Q9LE33; -.
DR BioCyc; ARA:AT1G12550-MON; -.
DR BioCyc; MetaCyc:AT1G12550-MON; -.
DR BRENDA; 1.1.1.81; 399.
DR PRO; PR:Q9LE33; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LE33; baseline and differential.
DR Genevisible; Q9LE33; AT.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IDA:TAIR.
DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IDA:TAIR.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0009854; P:oxidative photosynthetic carbon pathway; IEA:UniProtKB-KW.
DR GO; GO:0009853; P:photorespiration; IMP:TAIR.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
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.
PE 1: Evidence at protein level;
KW Glycolate pathway; NAD; NADP; Oxidoreductase; Photorespiration; Pyruvate;
KW Reference proteome.
FT CHAIN 1..323
FT /note="Glyoxylate/hydroxypyruvate reductase HPR3"
FT /id="PRO_0000419953"
FT ACT_SITE 240
FT /evidence="ECO:0000250"
FT ACT_SITE 269
FT /evidence="ECO:0000250"
FT ACT_SITE 287
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 160..163
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 182..184
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 238..240
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 287..289
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 323 AA; 34912 MW; 258FB419B9D67B9A CRC64;
MAESSEPPVV LLHRPPSLTF MDEILTREFR TLITDTSSSE SLPSFFPRHA SSARAFVISG
RLPVTDELLS HLPSLQILVC TSVGIDHIDL AACKRRGIVI TNAGNAFSDD VADCAVGLLI
SVLRRIPAAD RYVRSGNWAK FGDFQLGSKV SGKRVGIVGL GSIGSFVAKR LESFGCVISY
NSRSQKQSSP YRYYSDILSL AENNDVLVLC CSLTDETHHI VNREVMELLG KDGVVINVGR
GKLIDEKEMV KCLVDGVIGG AGLDVFENEP AVPQELFGLD NVVLSPHFAV ATPGSLDNVA
QIALANLKAF FSNRPLLSPV QLD
