P5CS2_ORYSJ
ID P5CS2_ORYSJ Reviewed; 735 AA.
AC Q941T1;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Delta-1-pyrroline-5-carboxylate synthase 2 {ECO:0000305};
DE Short=OsP5CS2 {ECO:0000303|Ref.7};
DE Includes:
DE RecName: Full=Glutamate 5-kinase;
DE Short=GK;
DE EC=2.7.2.11;
DE AltName: Full=Gamma-glutamyl kinase;
DE Includes:
DE RecName: Full=Gamma-glutamyl phosphate reductase;
DE Short=GPR;
DE EC=1.2.1.41;
DE AltName: Full=Glutamate-5-semialdehyde dehydrogenase;
DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase;
GN Name=P5CS2 {ECO:0000303|Ref.7};
GN OrderedLocusNames=Os01g0848200 {ECO:0000312|EMBL:BAF06716.1};
GN ORFNames=OsJ_04075 {ECO:0000312|EMBL:EEE55670.1},
GN P0005H10.23 {ECO:0000312|EMBL:BAB64280.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION.
RX DOI=10.3724/SP.J.1145.2014.03010;
RA Zhang X., Tang W., Liu J., Liu Y.;
RT "Co-expression of rice OsP5CS1 and OsP5CS2 genes in transgenic tobacco
RT resulted in elevated proline biosynthesis and enhanced abiotic stress
RT tolerance.";
RL Ying Yong Yu Huan Jing Sheng Wu Xue Bao 20:717-722(2014).
CC -!- FUNCTION: P5CS plays a key role in proline biosynthesis, leading to
CC osmoregulation in plants. Involved in abiotic stress tolerance.
CC {ECO:0000269|Ref.7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate = ADP + L-glutamyl 5-phosphate;
CC Xref=Rhea:RHEA:14877, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58274, ChEBI:CHEBI:456216; EC=2.7.2.11;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-
CC glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:19541,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58066, ChEBI:CHEBI:58274, ChEBI:CHEBI:58349; EC=1.2.1.41;
CC -!- ACTIVITY REGULATION: Feedback regulated by proline.
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 1/2.
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 2/2.
CC -!- MISCELLANEOUS: Tobacco plants over-expressing P5CS1 and P5CS2 have
CC elevated proline levels and display enhanced abiotic stress tolerance.
CC {ECO:0000269|Ref.7}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the glutamate 5-
CC kinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the gamma-glutamyl
CC phosphate reductase family. {ECO:0000305}.
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DR EMBL; AP004127; BAB64280.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF06716.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS75219.1; -; Genomic_DNA.
DR EMBL; CM000138; EEE55670.1; -; Genomic_DNA.
DR EMBL; AK101230; BAG94966.1; -; mRNA.
DR RefSeq; XP_015622203.1; XM_015766717.1.
DR AlphaFoldDB; Q941T1; -.
DR SMR; Q941T1; -.
DR STRING; 4530.OS01T0848200-02; -.
DR PaxDb; Q941T1; -.
DR PRIDE; Q941T1; -.
DR EnsemblPlants; Os01t0848200-01; Os01t0848200-01; Os01g0848200.
DR EnsemblPlants; Os01t0848200-02; Os01t0848200-02; Os01g0848200.
DR GeneID; 4324853; -.
DR Gramene; Os01t0848200-01; Os01t0848200-01; Os01g0848200.
DR Gramene; Os01t0848200-02; Os01t0848200-02; Os01g0848200.
DR KEGG; osa:4324853; -.
DR eggNOG; KOG1154; Eukaryota.
DR eggNOG; KOG4165; Eukaryota.
DR HOGENOM; CLU_016144_0_0_1; -.
DR InParanoid; Q941T1; -.
DR OMA; LHPEQRG; -.
DR OrthoDB; 832430at2759; -.
DR BRENDA; 1.2.1.41; 4460.
DR UniPathway; UPA00098; UER00359.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004349; F:glutamate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006561; P:proline biosynthetic process; IMP:UniProtKB.
DR CDD; cd07079; ALDH_F18-19_ProA-GPR; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR HAMAP; MF_00412; ProA; 1.
DR HAMAP; MF_00456; ProB; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR020593; G-glutamylP_reductase_CS.
DR InterPro; IPR001057; Glu/AcGlu_kinase.
DR InterPro; IPR005715; Glu_5kinase/COase_Synthase.
DR InterPro; IPR019797; Glutamate_5-kinase_CS.
DR InterPro; IPR000965; GPR_dom.
DR InterPro; IPR005766; P5_carboxy_syn.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036429; P5C_syn; 1.
DR PRINTS; PR00474; GLU5KINASE.
DR SUPFAM; SSF53633; SSF53633; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01092; P5CS; 1.
DR TIGRFAMs; TIGR00407; proA; 1.
DR TIGRFAMs; TIGR01027; proB; 1.
DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR PROSITE; PS01223; PROA; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; ATP-binding; Kinase; Multifunctional enzyme; NADP;
KW Nucleotide-binding; Oxidoreductase; Proline biosynthesis;
KW Reference proteome; Stress response; Transferase.
FT CHAIN 1..735
FT /note="Delta-1-pyrroline-5-carboxylate synthase 2"
FT /id="PRO_0000439825"
FT REGION 1..315
FT /note="Glutamate 5-kinase"
FT REGION 316..735
FT /note="Gamma-glutamyl phosphate reductase"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A7B5"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A7B5"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A7B5"
FT BINDING 215..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9PJ29"
FT BINDING 221..226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9PJ29"
FT BINDING 255..261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9PJ29"
SQ SEQUENCE 735 AA; 79508 MW; C14C53D50B63B572 CRC64;
MGRGGIGGAG LVAAVAKADV ENTDSTRGFV KDVKRIIIKV GTAVVTGPNG RLAMGRLGAL
CEQVKQLNFE GYEVILVTSG AVGVGRQRLK YRKLVNSSFA DLQNPQMDMD GKACAAVGQS
VLMAIYDTLF SQLDVTSSQL LVTDRDFMDP SFGNQLRETV NSLLDLKVIP VFNENDAIST
RRQPYEDSSG IFWDNDSLAR LLAQELKADL LIMLSDVEGL YSGPPSDPQS KIIHTYVHEQ
HGKLISFGEK SRVGRGGMQA KVAAAFTASS KGIPVVIASG FAIDSIIKVM RGEKIGTLFH
REANQWGCSK EATAREMAVA ARDCSRHLQK LSSEERKKIL LDIADALEAN EDLITSENQA
DLDLAQDIGY DKSLVARMTI KPGKIKSLAG SIREIADMED PISHTLKRTE VAKDLVFEKT
YCPLGVLLII FESRPDALVQ IASLAIRSGN GLLLKGGKEA MRSNTILHKV ITGAIPDVVG
KKLIGLVKNK DEIADLLKLD DVIDLVIPRG SNKLVSQIKA ATKIPVLGHA DGICHVYIDK
SADMDMAKRI VLDAKVDYPA ACNAMETLLV HKDLNRTEGL DDLLVELEKE GVVIYGGPVA
HDTLKLPKVD SFHHEYNSMA CTLEFVDDVQ SAIDHINRYG SAHTDCIITT DGKAAETFLQ
QVDSAAVFHN ASTRFCDGAR FGLGAEVGIS TGRIHARGPV GVDGLLTTRC ILRGSGQVVN
GDKGVVYTHR ELPLQ
