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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
 
 
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