ID   P5CS1_ORYSJ             Reviewed;         716 AA.
AC   O04226; Q0DHN6; Q60EM4; Q6PW76;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Delta-1-pyrroline-5-carboxylate synthase 1 {ECO:0000305};
DE            Short=OsP5CS1 {ECO:0000303|Ref.8};
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=P5CS1 {ECO:0000303|Ref.8};
GN   Synonyms=P5CS {ECO:0000303|PubMed:9106509};
GN   OrderedLocusNames=Os05g0455500, LOC_Os05g38150; ORFNames=OJ1651_D06.9;
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 [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Akibare;
RX   PubMed=9106509; DOI=10.1023/a:1005702408601;
RA   Igarashi Y., Yoshiba Y., Sanada Y., Yamaguchi-Shinozaki K., Wada K.,
RA   Shinozaki K.;
RT   "Characterization of the gene for delta1-pyrroline-5-carboxylate synthetase
RT   and correlation between the expression of the gene and salt tolerance in
RT   Oryza sativa L.";
RL   Plant Mol. Biol. 33:857-865(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Tainung 71;
RA   Huang T.-C., Chuang H.-S., Yen T.-Y., Huang Y.-W., Wu M.-L.;
RT   "Nucleotide sequence of delta-1-pyrroline-5-carboxylate synthetase.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA   Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA   Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA   Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT   "A fine physical map of the rice chromosome 5.";
RL   Mol. Genet. Genomics 274:337-345(2005).
RN   [4]
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   [5]
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   [6]
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   [7]
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   [8]
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.8}.
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   -!- TISSUE SPECIFICITY: Expressed at high levels in leaves.
CC       {ECO:0000269|PubMed:9106509}.
CC   -!- INDUCTION: Induced by salt, drought and cold stresses, and abscisic
CC       acid (ABA). {ECO:0000269|PubMed:9106509}.
CC   -!- MISCELLANEOUS: Tobacco plants over-expressing P5CS1 and P5CS2 have
CC       elevated proline levels and display enhanced abiotic stress tolerance.
CC       {ECO:0000269|Ref.8}.
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; D49714; BAA19916.1; -; mRNA.
DR   EMBL; AY574031; AAS89034.1; -; mRNA.
DR   EMBL; AC111016; AAU90213.1; -; Genomic_DNA.
DR   EMBL; AP008211; BAF17637.1; -; Genomic_DNA.
DR   EMBL; AP014961; BAS94357.1; -; Genomic_DNA.
DR   EMBL; AK102633; BAG95649.1; -; mRNA.
DR   PIR; T03695; T03695.
DR   RefSeq; XP_015640176.1; XM_015784690.1.
DR   AlphaFoldDB; O04226; -.
DR   SMR; O04226; -.
DR   STRING; 39947.O04226; -.
DR   PaxDb; 39947-O04226; -.
DR   EnsemblPlants; Os05t0455500-02; Os05t0455500-02; Os05g0455500.
DR   GeneID; 4338979; -.
DR   Gramene; Os05t0455500-02; Os05t0455500-02; Os05g0455500.
DR   KEGG; osa:4338979; -.
DR   eggNOG; KOG1154; Eukaryota.
DR   eggNOG; KOG4165; Eukaryota.
DR   HOGENOM; CLU_016144_0_0_1; -.
DR   InParanoid; O04226; -.
DR   OMA; MGHAEGI; -.
DR   OrthoDB; 314297at2759; -.
DR   BRENDA; 1.2.1.88; 4460.
DR   PlantReactome; R-OSA-1119495; Citrulline biosynthesis.
DR   PlantReactome; R-OSA-1119631; Proline biosynthesis I.
DR   UniPathway; UPA00098; UER00359.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000000763; Chromosome 5.
DR   Proteomes; UP000059680; Chromosome 5.
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; cd04256; AAK_P5CS_ProBA; 1.
DR   CDD; cd07079; ALDH_F18-19_ProA-GPR; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 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; IPR041744; G5K_ProBA.
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   NCBIfam; TIGR01092; P5CS; 1.
DR   NCBIfam; TIGR00407; proA; 1.
DR   NCBIfam; TIGR01027; proB; 1.
DR   PANTHER; PTHR11063:SF8; DELTA-1-PYRROLINE-5-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR11063; GLUTAMATE SEMIALDEHYDE DEHYDROGENASE; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036429; P5C_syn; 1.
DR   PRINTS; PR00474; GLU5KINASE.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR   PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR   PROSITE; PS01223; PROA; 1.
DR   Genevisible; O04226; OS.
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..716
FT                   /note="Delta-1-pyrroline-5-carboxylate synthase 1"
FT                   /id="PRO_0000109777"
FT   REGION          1..296
FT                   /note="Glutamate 5-kinase"
FT   REGION          297..716
FT                   /note="Gamma-glutamyl phosphate reductase"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A7B5"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A7B5"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A7B5"
FT   BINDING         196..197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9PJ29"
FT   BINDING         202..207
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9PJ29"
FT   BINDING         236..242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9PJ29"
FT   CONFLICT        173
FT                   /note="F -> S (in Ref. 2; AAS89034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        488
FT                   /note="I -> T (in Ref. 1; BAA19916)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        500
FT                   /note="K -> E (in Ref. 2; AAS89034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        530
FT                   /note="H -> L (in Ref. 1; BAA19916)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        537
FT                   /note="I -> T (in Ref. 1; BAA19916)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   716 AA;  77745 MW;  F8D3C7D9449CFA64 CRC64;
     MASVDPSRSF VRDVKRVIIK VGTAVVSRQD GRLALGRVGA LCEQVKELNS LGYEVILVTS
     GAVGVGRQRL RYRKLVNSSF ADLQKPQMEL DGKACAAVGQ SGLMALYDML FNQLDVSSSQ
     LLVTDSDFEN PKFREQLTET VESLLDLKVI PIFNENDAIS TRKAPYEDSS GIFWDNDSLA
     GLLALELKAD LLILLSDVDG LYSGPPSEPS SKIIHTYIKE KHQQEITFGD KSRVGRGGMT
     AKVKAAVLAS NSGTPVVITS GFENRSILKV LHGEKIGTLF HKNANLWESS KDVSTREMAV
     AARDCSRHLQ NLSSEERKKI LLDVADALEA NEDLIRSENE ADVAAAQVAG YEKPLVARLT
     IKPGKIASLA KSIRTLANME DPINQILKKT EVADDLVLEK TSCPLGVLLI VFESRPDALV
     QIASLAIRSG NGLLLKGGKE AIRSNTILHK VITDAIPRNV GEKLIGLVTT RDEIADLLKL
     DDVIDLVIPR GSNKLVSQIK ASTKIPVLGH ADGICHVYID KSADMDMAKH IVMDAKIDYP
     AACNAMETLL VHKDLMKSPG LDDILVALKT EGVNIYGGPI AHKALGFPKA VSFHHEYSSM
     ACTVEFVDDV QSAIDHIHRY GSAHTDCIVT TDDKVAETFL RRVDSAAVFH NASTRFSDGA
     RFGLGAEVGI STGRIHARGP VGVEGLLTTR WILRGRGQVV NGDKDVVYTH KSLPLQ
//