P5CS1_ARATH
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 03-AUG-2022, entry version 164.
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; 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=10.1111/j.0960-7412.1997.00557.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.AT2G39800.1; -.
DR iPTMnet; P54887; -.
DR PaxDb; P54887; -.
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; locus:2063907; AT2G39800.
DR eggNOG; KOG1154; Eukaryota.
DR eggNOG; KOG4165; Eukaryota.
DR InParanoid; P54887; -.
DR PhylomeDB; P54887; -.
DR BioCyc; ARA:AT2G39800-MON; -.
DR BioCyc; MetaCyc:AT2G39800-MON; -.
DR UniPathway; UPA00098; UER00359.
DR UniPathway; UPA00098; UER00360.
DR PRO; PR:P54887; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P54887; baseline and differential.
DR Genevisible; P54887; AT.
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; IBA:GO_Central.
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; -; 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 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
