GLYR2_ARATH
ID GLYR2_ARATH Reviewed; 358 AA.
AC F4I907; Q8RWF1;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Glyoxylate/succinic semialdehyde reductase 2, chloroplastic;
DE Short=AtGLYR2;
DE Short=AtGR2;
DE Short=SSA reductase 2;
DE EC=1.1.1.79 {ECO:0000269|PubMed:18495639};
DE EC=1.1.1.n11 {ECO:0000269|PubMed:18495639};
DE Flags: Precursor;
GN Name=GLYR2; Synonyms=GR2; OrderedLocusNames=At1g17650; ORFNames=F11A6.12;
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] OF 6-358.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-358 AND 16-358.
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18495639; DOI=10.1093/jxb/ern123;
RA Simpson J.P., Di Leo R., Dhanoa P.K., Allan W.L., Makhmoudova A.,
RA Clark S.M., Hoover G.J., Mullen R.T., Shelp B.J.;
RT "Identification and characterization of a plastid-localized Arabidopsis
RT glyoxylate reductase isoform: comparison with a cytosolic isoform and
RT implications for cellular redox homeostasis and aldehyde detoxification.";
RL J. Exp. Bot. 59:2545-2554(2008).
RN [6]
RP INDUCTION.
RX PubMed=18495640; DOI=10.1093/jxb/ern122;
RA Allan W.L., Simpson J.P., Clark S.M., Shelp B.J.;
RT "Gamma-hydroxybutyrate accumulation in Arabidopsis and tobacco plants is a
RT general response to abiotic stress: putative regulation by redox balance
RT and glyoxylate reductase isoforms.";
RL J. Exp. Bot. 59:2555-2564(2008).
RN [7]
RP INDUCTION.
RX PubMed=19453511; DOI=10.1111/j.1399-3054.2009.01220.x;
RA Yoshida S., Tamaoki M., Ioki M., Ogawa D., Sato Y., Aono M., Kubo A.,
RA Saji S., Saji H., Satoh S., Nakajima N.;
RT "Ethylene and salicylic acid control glutathione biosynthesis in ozone-
RT exposed Arabidopsis thaliana.";
RL Physiol. Plantarum 136:284-298(2009).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate to
CC glycolate as well as succinic semialdehyde (SSA) to gamma-
CC hydroxybutyrate in vitro. May function in redox homeostasis and play a
CC role in oxidative stress tolerance by detoxifying glyoxylate and SSA
CC generated in glycolate metabolism and GABA metabolism, respectively.
CC {ECO:0000269|PubMed:18495639}.
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:18495639};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybutanoate + NADP(+) = H(+) + NADPH + succinate
CC semialdehyde; Xref=Rhea:RHEA:26381, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16724, ChEBI:CHEBI:57706, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.1.1.n11;
CC Evidence={ECO:0000269|PubMed:18495639};
CC -!- ACTIVITY REGULATION: The ratio of NADPH/NADP(+) may regulate enzymatic
CC activity. {ECO:0000305}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=34 uM for glyoxylate (check for NADPH)
CC {ECO:0000269|PubMed:18495639};
CC KM=8.96 mM for succinate semialdehyde {ECO:0000269|PubMed:18495639};
CC KM=34 uM for NADPH (in the presence of glyoxylate as cosubstrate)
CC {ECO:0000269|PubMed:18495639};
CC KM=12 uM for NADPH (in the presence of succinate semialdehyde as
CC cosubstrate) {ECO:0000269|PubMed:18495639};
CC Vmax=40.6 umol/min/mg enzyme toward glyoxylate
CC {ECO:0000269|PubMed:18495639};
CC Vmax=30.7 umol/min/mg enzyme toward succinate semialdehyde
CC {ECO:0000269|PubMed:18495639};
CC pH dependence:
CC Optimum pH is 6.8-7.8. {ECO:0000269|PubMed:18495639};
CC -!- INTERACTION:
CC F4I907; Q9LPR8: SCL3; NbExp=3; IntAct=EBI-4453651, EBI-4429250;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000305|PubMed:18495639}.
CC -!- INDUCTION: By cold and heat stresses. Down-regulated by ozone.
CC {ECO:0000269|PubMed:18495640, ECO:0000269|PubMed:19453511}.
CC -!- MISCELLANEOUS: Although GLYR2 acts as an aldo/keto reductase, it has no
CC significant homology with either mammalian and bacterial NADPH-
CC dependent SSA reductases.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. NP60 subfamily.
CC {ECO:0000305}.
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DR EMBL; AC034257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE29618.1; -; Genomic_DNA.
DR EMBL; AY085690; AAM62909.1; -; mRNA.
DR EMBL; AY093135; AAM13134.1; -; mRNA.
DR EMBL; BT008734; AAP42747.1; -; mRNA.
DR RefSeq; NP_564030.2; NM_101628.4.
DR AlphaFoldDB; F4I907; -.
DR SMR; F4I907; -.
DR BioGRID; 23582; 7.
DR IntAct; F4I907; 2.
DR STRING; 3702.AT1G17650.1; -.
DR MetOSite; F4I907; -.
DR PaxDb; F4I907; -.
DR PRIDE; F4I907; -.
DR ProteomicsDB; 248531; -.
DR EnsemblPlants; AT1G17650.1; AT1G17650.1; AT1G17650.
DR GeneID; 838342; -.
DR Gramene; AT1G17650.1; AT1G17650.1; AT1G17650.
DR KEGG; ath:AT1G17650; -.
DR Araport; AT1G17650; -.
DR TAIR; locus:2007923; AT1G17650.
DR eggNOG; KOG0409; Eukaryota.
DR HOGENOM; CLU_035117_0_0_1; -.
DR InParanoid; F4I907; -.
DR OrthoDB; 812358at2759; -.
DR BRENDA; 1.1.1.79; 399.
DR SABIO-RK; F4I907; -.
DR PRO; PR:F4I907; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I907; baseline and differential.
DR Genevisible; F4I907; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IDA:TAIR.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP 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 Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029154; NADP-bd.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Chloroplast; NAD; NADP; Oxidoreductase; Plastid; Reference proteome;
KW Stress response; Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..358
FT /note="Glyoxylate/succinic semialdehyde reductase 2,
FT chloroplastic"
FT /id="PRO_0000421033"
FT ACT_SITE 236
FT /evidence="ECO:0000250"
FT BINDING 70..84
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT BINDING 161
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT BINDING 304
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
SQ SEQUENCE 358 AA; 37781 MW; C46D7A0338B5BF3B CRC64;
MPLVSLSFAS SSSKAMALCS ICPRIPLRFR PKPISPFLSK PQICLAYRVY SSLQSTTPST
RDELGTVSIG FLGMGIMGSP MAQNLIKAGC DVTVWNRTKS KCDPLVGLGA KYKSSPEEVT
ATCDLTFAML ADPESAIDVA CGKNGAIFGI SSGKGYVDVS TVDVASSILI SKQIKDTGAL
FLEAPVSGSK KPAEDGQLIF LTAGDKPLYE KAAPFLDIMG KSKFYLGEVG NGAAMKLVVN
MIMGSMMASF AEGILLSQKV GLDPNVLVEV VSQGAINAPM YSLKGPSMIK SVYPTAFPLK
HQQKDMRLAL GLAESVSQST PIAAAANELY KVAKSYGLSD EDFSAVIEAL KAAKSREA
