GenomeNet

Database: UniProt
Entry: F4I907
LinkDB: F4I907
Original site: F4I907 
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   16-JAN-2019, entry version 62.
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;
GN   ORFNames=F11A6.12;
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] 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.,
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   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
RT   Arabidopsis glyoxylate reductase isoform: comparison with a cytosolic
RT   isoform and implications for cellular redox homeostasis and aldehyde
RT   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
RT   is a general response to abiotic stress: putative regulation by redox
RT   balance 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
RT   ozone-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
CC       play a role in oxidative stress tolerance by detoxifying
CC       glyoxylate and SSA generated in glycolate metabolism and GABA
CC       metabolism, respectively. {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;
CC         EC=1.1.1.79; 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
CC       enzymatic 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
CC         {ECO:0000269|PubMed:18495639};
CC         KM=34 uM for NADPH (in the presence of glyoxylate as
CC         cosubstrate) {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   -!- 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
CC       has no significant homology with either mammalian and bacterial
CC       NADPH-dependent SSA reductases.
CC   -!- SIMILARITY: Belongs to the HIBADH-related family. NP60 subfamily.
CC       {ECO:0000305}.
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   UniGene; At.41821; -.
DR   ProteinModelPortal; F4I907; -.
DR   SMR; F4I907; -.
DR   BioGrid; 23582; 1.
DR   IntAct; F4I907; 1.
DR   STRING; 3702.AT1G17650.1; -.
DR   PaxDb; F4I907; -.
DR   PRIDE; F4I907; -.
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   eggNOG; COG2084; LUCA.
DR   HOGENOM; HOG000219608; -.
DR   InParanoid; F4I907; -.
DR   KO; K18121; -.
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; IDA: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   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; Complete proteome; NAD; NADP; Oxidoreductase; Plastid;
KW   Reference proteome; Stress response; Transit peptide.
FT   TRANSIT       1     44       Chloroplast. {ECO:0000255}.
FT   CHAIN        45    358       Glyoxylate/succinic semialdehyde
FT                                reductase 2, chloroplastic.
FT                                /FTId=PRO_0000421033.
FT   NP_BIND      70     84       NADP. {ECO:0000250|UniProtKB:Q49A26}.
FT   ACT_SITE    236    236       {ECO:0000250}.
FT   BINDING     161    161       NADP. {ECO:0000250|UniProtKB:Q49A26}.
FT   BINDING     304    304       NADP. {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
//
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