P5CS1_ORYSJ
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 03-AUG-2022, entry version 152.
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}; 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; 4530.OS05T0455500-02; -.
DR PaxDb; O04226; -.
DR PRIDE; 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; EGRECIM; -.
DR OrthoDB; 832430at2759; -.
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 Genevisible; O04226; OS.
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; -; 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; 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 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..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
