ID   P5CS1_ARATH             Reviewed;         717 AA.
AC   P54887;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 170.
DE   RecName: Full=Delta-1-pyrroline-5-carboxylate synthase A;
DE            Short=P5CS A;
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=P5CSA; Synonyms=P5CS1; OrderedLocusNames=At2g39800;
GN   ORFNames=T5I7.10;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=7556633; DOI=10.1016/0014-5793(95)00935-3;
RA   Savoure A., Jaoua S., Hua X.J., Ardiles W., van Montagu M., Verbruggen N.;
RT   "Isolation, characterization, and chromosomal location of a gene encoding
RT   the delta 1-pyrroline-5-carboxylate synthetase in Arabidopsis thaliana.";
RL   FEBS Lett. 372:13-19(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9351242; DOI=10.1046/j.1365-313x.1997.00557.x;
RA   Strizhov N., Abraham E., Oekresz L., Blickling S., Zilberstein A.,
RA   Schell J., Koncz C., Szabados L.;
RT   "Differential expression of two P5CS genes controlling proline accumulation
RT   during salt-stress requires ABA and is regulated by ABA1, ABI1 and AXR2 in
RT   Arabidopsis.";
RL   Plant J. 12:557-569(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=7773306; DOI=10.1046/j.1365-313x.1995.07050751.x;
RA   Yoshiba Y., Kiyosue T., Katagiri T., Ueda H., Mizoguchi T.,
RA   Yamaguchi-Shinozaki K., Wada K., Harada Y., Shinozaki K.;
RT   "Correlation between the induction of a gene for delta 1-pyrroline-5-
RT   carboxylate synthetase and the accumulation of proline in Arabidopsis
RT   thaliana under osmotic stress.";
RL   Plant J. 7:751-760(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [5]
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 reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
CC   -!- FUNCTION: P5CS plays a key role in proline biosynthesis, leading to
CC       osmoregulation in plants.
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   -!- 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=P54887-1; Sequence=Displayed;
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; X89414; CAA61593.1; -; Genomic_DNA.
DR   EMBL; X86777; CAA60446.1; -; mRNA.
DR   EMBL; X87330; CAA60740.1; -; mRNA.
DR   EMBL; D32138; BAA06864.1; -; mRNA.
DR   EMBL; AC003000; AAB87129.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09729.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09730.1; -; Genomic_DNA.
DR   EMBL; AF424633; AAL11626.1; -; mRNA.
DR   EMBL; AY113046; AAM47354.1; -; mRNA.
DR   EMBL; AY150430; AAN12972.1; -; mRNA.
DR   PIR; S66637; S66637.
DR   PIR; T50685; T50685.
DR   RefSeq; NP_001189714.1; NM_001202785.1. [P54887-1]
DR   RefSeq; NP_181510.1; NM_129539.2. [P54887-1]
DR   AlphaFoldDB; P54887; -.
DR   SMR; P54887; -.
DR   BioGRID; 3904; 6.
DR   IntAct; P54887; 6.
DR   STRING; 3702.P54887; -.
DR   iPTMnet; P54887; -.
DR   PaxDb; 3702-AT2G39800-1; -.
DR   EnsemblPlants; AT2G39800.1; AT2G39800.1; AT2G39800. [P54887-1]
DR   EnsemblPlants; AT2G39800.4; AT2G39800.4; AT2G39800. [P54887-1]
DR   GeneID; 818566; -.
DR   Gramene; AT2G39800.1; AT2G39800.1; AT2G39800. [P54887-1]
DR   Gramene; AT2G39800.4; AT2G39800.4; AT2G39800. [P54887-1]
DR   KEGG; ath:AT2G39800; -.
DR   Araport; AT2G39800; -.
DR   TAIR; AT2G39800; P5CS1.
DR   eggNOG; KOG1154; Eukaryota.
DR   eggNOG; KOG4165; Eukaryota.
DR   InParanoid; P54887; -.
DR   OrthoDB; 314297at2759; -.
DR   PhylomeDB; P54887; -.
DR   BioCyc; ARA:AT2G39800-MONOMER; -.
DR   BioCyc; MetaCyc:AT2G39800-MONOMER; -.
DR   UniPathway; UPA00098; UER00359.
DR   UniPathway; UPA00098; UER00360.
DR   PRO; PR:P54887; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P54887; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017084; F:delta1-pyrroline-5-carboxylate synthetase activity; ISS:TAIR.
DR   GO; GO:0004349; F:glutamate 5-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042538; P:hyperosmotic salinity response; IMP:TAIR.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009555; P:pollen development; IMP:TAIR.
DR   GO; GO:0006561; P:proline biosynthetic process; IMP:TAIR.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR   GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR   GO; GO:0009414; P:response to water deprivation; IGI:TAIR.
DR   GO; GO:0048364; P:root development; IMP:TAIR.
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; 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:SF20; DELTA-1-PYRROLINE-5-CARBOXYLATE SYNTHASE A; 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; P54887; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Amino-acid biosynthesis; ATP-binding; Kinase;
KW   Multifunctional enzyme; NADP; Nucleotide-binding; Oxidoreductase;
KW   Proline biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..717
FT                   /note="Delta-1-pyrroline-5-carboxylate synthase A"
FT                   /id="PRO_0000109772"
FT   REGION          1..296
FT                   /note="Glutamate 5-kinase"
FT   REGION          297..717
FT                   /note="Gamma-glutamyl phosphate reductase"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         196..197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         236..242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        42
FT                   /note="C -> F (in Ref. 3; BAA06864)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        54
FT                   /note="E -> K (in Ref. 3; BAA06864)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        381
FT                   /note="D -> E (in Ref. 3; BAA06864)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        467
FT                   /note="L -> F (in Ref. 3; BAA06864)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        676
FT                   /note="H -> Y (in Ref. 3; BAA06864)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   717 AA;  77702 MW;  DF2B296362351A78 CRC64;
     MEELDRSRAF ARDVKRIVVK VGTAVVTGKG GRLALGRLGA LCEQLAELNS DGFEVILVSS
     GAVGLGRQRL RYRQLVNSSF ADLQKPQTEL DGKACAGVGQ SSLMAYYETM FDQLDVTAAQ
     LLVNDSSFRD KDFRKQLNET VKSMLDLRVI PIFNENDAIS TRRAPYQDSS GIFWDNDSLA
     ALLALELKAD LLILLSDVEG LYTGPPSDPN SKLIHTFVKE KHQDEITFGD KSRLGRGGMT
     AKVKAAVNAA YAGIPVIITS GYSAENIDKV LRGLRVGTLF HQDARLWAPI TDSNARDMAV
     AARESSRKLQ ALSSEDRKKI LLDIADALEA NVTTIKAENE LDVASAQEAG LEESMVARLV
     MTPGKISSLA ASVRKLADME DPIGRVLKKT EVADGLVLEK TSSPLGVLLI VFESRPDALV
     QIASLAIRSG NGLLLKGGKE ARRSNAILHK VITDAIPETV GGKLIGLVTS REEIPDLLKL
     DDVIDLVIPR GSNKLVTQIK NTTKIPVLGH ADGICHVYVD KACDTDMAKR IVSDAKLDYP
     AACNAMETLL VHKDLEQNAV LNELIFALQS NGVTLYGGPR ASKILNIPEA RSFNHEYCAK
     ACTVEVVEDV YGAIDHIHRH GSAHTDCIVT EDHEVAELFL RQVDSAAVFH NASTRFSDGF
     RFGLGAEVGV STGRIHARGP VGVEGLLTTR WIMRGKGQVV DGDNGIVYTH QDIPIQA
//