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Protein

Delta-1-pyrroline-5-carboxylate synthase A

Gene

P5CSA

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

P5CS plays a key role in proline biosynthesis, leading to osmoregulation in plants.

Catalytic activityi

ATP + L-glutamate = ADP + L-glutamate 5-phosphate.
L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH.

Pathway: L-proline biosynthesis

This protein is involved in step 1 and 2 of the subpathway that synthesizes L-glutamate 5-semialdehyde from L-glutamate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Delta-1-pyrroline-5-carboxylate synthase B (P5CSB), Delta-1-pyrroline-5-carboxylate synthase A (P5CSA)
  2. Delta-1-pyrroline-5-carboxylate synthase B (P5CSB), Delta-1-pyrroline-5-carboxylate synthase A (P5CSA)
This subpathway is part of the pathway L-proline biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate 5-semialdehyde from L-glutamate, the pathway L-proline biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601SubstrateBy similarity
Binding sitei157 – 1571SubstrateBy similarity
Binding sitei176 – 1761Substrate; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi196 – 1972ATPBy similarity
Nucleotide bindingi236 – 2427ATPBy similarity

GO - Molecular functioni

GO - Biological processi

  • hyperosmotic salinity response Source: TAIR
  • L-proline biosynthetic process Source: UniProtKB-UniPathway
  • pollen development Source: TAIR
  • proline biosynthetic process Source: TAIR
  • response to oxidative stress Source: TAIR
  • response to salt stress Source: TAIR
  • response to water deprivation Source: TAIR
  • root development Source: TAIR

Keywords - Molecular functioni

Kinase, Oxidoreductase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Proline biosynthesis

Keywords - Ligandi

ATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT2G39800-MONOMER.
ARA:GQT-2788-MONOMER.
ARA:GQT-2789-MONOMER.
ARA:GQT-2790-MONOMER.
MetaCyc:AT2G39800-MONOMER.
ReactomeiREACT_276185. Amino acid synthesis and interconversion (transamination).
UniPathwayiUPA00098; UER00359.
UPA00098; UER00360.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-1-pyrroline-5-carboxylate synthase A
Short name:
P5CS A
Including the following 2 domains:
Glutamate 5-kinase (EC:2.7.2.11)
Short name:
GK
Alternative name(s):
Gamma-glutamyl kinase
Gamma-glutamyl phosphate reductase (EC:1.2.1.41)
Short name:
GPR
Alternative name(s):
Glutamate-5-semialdehyde dehydrogenase
Glutamyl-gamma-semialdehyde dehydrogenase
Gene namesi
Name:P5CSA
Synonyms:P5CS1
Ordered Locus Names:At2g39800
ORF Names:T5I7.10
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G39800.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • cytoplasm Source: TAIR
  • membrane Source: TAIR

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 717717Delta-1-pyrroline-5-carboxylate synthase APRO_0000109772Add
BLAST

Proteomic databases

PaxDbiP54887.
PRIDEiP54887.

Expressioni

Gene expression databases

ExpressionAtlasiP54887. baseline and differential.

Interactioni

Protein-protein interaction databases

BioGridi3904. 6 interactions.
IntActiP54887. 6 interactions.
STRINGi3702.AT2G39800.1.

Structurei

3D structure databases

ProteinModelPortaliP54887.
SMRiP54887. Positions 13-284, 302-715.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 296296Glutamate 5-kinaseAdd
BLAST
Regioni297 – 717421Gamma-glutamyl phosphate reductaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the glutamate 5-kinase family.Curated
In the C-terminal section; belongs to the gamma-glutamyl phosphate reductase family.Curated

Phylogenomic databases

eggNOGiCOG0014.
HOGENOMiHOG000246357.
InParanoidiP54887.
KOiK12657.
OMAiFEARPDC.
PhylomeDBiP54887.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPiMF_00412. ProA.
MF_00456. ProB.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR020593. G-glutamylP_reductase_CS.
IPR001057. Glu/AcGlu_kinase.
IPR005715. Glu_5kinase/COase_Synthase.
IPR019797. Glutamate_5-kinase_CS.
IPR000965. GPR_dom.
IPR005766. P5_carboxy_syn.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFiPIRSF036429. P5C_syn. 1 hit.
PRINTSiPR00474. GLU5KINASE.
SUPFAMiSSF53633. SSF53633. 1 hit.
SSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01092. P5CS. 1 hit.
TIGR00407. proA. 1 hit.
TIGR01027. proB. 1 hit.
PROSITEiPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS01223. PROA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P54887-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEELDRSRAF ARDVKRIVVK VGTAVVTGKG GRLALGRLGA LCEQLAELNS
60 70 80 90 100
DGFEVILVSS GAVGLGRQRL RYRQLVNSSF ADLQKPQTEL DGKACAGVGQ
110 120 130 140 150
SSLMAYYETM FDQLDVTAAQ LLVNDSSFRD KDFRKQLNET VKSMLDLRVI
160 170 180 190 200
PIFNENDAIS TRRAPYQDSS GIFWDNDSLA ALLALELKAD LLILLSDVEG
210 220 230 240 250
LYTGPPSDPN SKLIHTFVKE KHQDEITFGD KSRLGRGGMT AKVKAAVNAA
260 270 280 290 300
YAGIPVIITS GYSAENIDKV LRGLRVGTLF HQDARLWAPI TDSNARDMAV
310 320 330 340 350
AARESSRKLQ ALSSEDRKKI LLDIADALEA NVTTIKAENE LDVASAQEAG
360 370 380 390 400
LEESMVARLV MTPGKISSLA ASVRKLADME DPIGRVLKKT EVADGLVLEK
410 420 430 440 450
TSSPLGVLLI VFESRPDALV QIASLAIRSG NGLLLKGGKE ARRSNAILHK
460 470 480 490 500
VITDAIPETV GGKLIGLVTS REEIPDLLKL DDVIDLVIPR GSNKLVTQIK
510 520 530 540 550
NTTKIPVLGH ADGICHVYVD KACDTDMAKR IVSDAKLDYP AACNAMETLL
560 570 580 590 600
VHKDLEQNAV LNELIFALQS NGVTLYGGPR ASKILNIPEA RSFNHEYCAK
610 620 630 640 650
ACTVEVVEDV YGAIDHIHRH GSAHTDCIVT EDHEVAELFL RQVDSAAVFH
660 670 680 690 700
NASTRFSDGF RFGLGAEVGV STGRIHARGP VGVEGLLTTR WIMRGKGQVV
710
DGDNGIVYTH QDIPIQA
Length:717
Mass (Da):77,702
Last modified:October 1, 1996 - v1
Checksum:iDF2B296362351A78
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421C → F in BAA06864 (PubMed:7773306).Curated
Sequence conflicti54 – 541E → K in BAA06864 (PubMed:7773306).Curated
Sequence conflicti381 – 3811D → E in BAA06864 (PubMed:7773306).Curated
Sequence conflicti467 – 4671L → F in BAA06864 (PubMed:7773306).Curated
Sequence conflicti676 – 6761H → Y in BAA06864 (PubMed:7773306).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89414 Genomic DNA. Translation: CAA61593.1.
X86777 mRNA. Translation: CAA60446.1.
X87330 mRNA. Translation: CAA60740.1.
D32138 mRNA. Translation: BAA06864.1.
AC003000 Genomic DNA. Translation: AAB87129.1.
CP002685 Genomic DNA. Translation: AEC09729.1.
CP002685 Genomic DNA. Translation: AEC09730.1.
AF424633 mRNA. Translation: AAL11626.1.
AY113046 mRNA. Translation: AAM47354.1.
AY150430 mRNA. Translation: AAN12972.1.
PIRiS66637.
T50685.
RefSeqiNP_001189714.1. NM_001202785.1. [P54887-1]
NP_181510.1. NM_129539.2. [P54887-1]
UniGeneiAt.20482.

Genome annotation databases

EnsemblPlantsiAT2G39800.1; AT2G39800.1; AT2G39800. [P54887-1]
AT2G39800.4; AT2G39800.4; AT2G39800. [P54887-1]
GeneIDi818566.
KEGGiath:AT2G39800.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89414 Genomic DNA. Translation: CAA61593.1.
X86777 mRNA. Translation: CAA60446.1.
X87330 mRNA. Translation: CAA60740.1.
D32138 mRNA. Translation: BAA06864.1.
AC003000 Genomic DNA. Translation: AAB87129.1.
CP002685 Genomic DNA. Translation: AEC09729.1.
CP002685 Genomic DNA. Translation: AEC09730.1.
AF424633 mRNA. Translation: AAL11626.1.
AY113046 mRNA. Translation: AAM47354.1.
AY150430 mRNA. Translation: AAN12972.1.
PIRiS66637.
T50685.
RefSeqiNP_001189714.1. NM_001202785.1. [P54887-1]
NP_181510.1. NM_129539.2. [P54887-1]
UniGeneiAt.20482.

3D structure databases

ProteinModelPortaliP54887.
SMRiP54887. Positions 13-284, 302-715.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi3904. 6 interactions.
IntActiP54887. 6 interactions.
STRINGi3702.AT2G39800.1.

Proteomic databases

PaxDbiP54887.
PRIDEiP54887.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G39800.1; AT2G39800.1; AT2G39800. [P54887-1]
AT2G39800.4; AT2G39800.4; AT2G39800. [P54887-1]
GeneIDi818566.
KEGGiath:AT2G39800.

Organism-specific databases

TAIRiAT2G39800.

Phylogenomic databases

eggNOGiCOG0014.
HOGENOMiHOG000246357.
InParanoidiP54887.
KOiK12657.
OMAiFEARPDC.
PhylomeDBiP54887.

Enzyme and pathway databases

UniPathwayiUPA00098; UER00359.
UPA00098; UER00360.
BioCyciARA:AT2G39800-MONOMER.
ARA:GQT-2788-MONOMER.
ARA:GQT-2789-MONOMER.
ARA:GQT-2790-MONOMER.
MetaCyc:AT2G39800-MONOMER.
ReactomeiREACT_276185. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

PROiP54887.

Gene expression databases

ExpressionAtlasiP54887. baseline and differential.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPiMF_00412. ProA.
MF_00456. ProB.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR020593. G-glutamylP_reductase_CS.
IPR001057. Glu/AcGlu_kinase.
IPR005715. Glu_5kinase/COase_Synthase.
IPR019797. Glutamate_5-kinase_CS.
IPR000965. GPR_dom.
IPR005766. P5_carboxy_syn.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFiPIRSF036429. P5C_syn. 1 hit.
PRINTSiPR00474. GLU5KINASE.
SUPFAMiSSF53633. SSF53633. 1 hit.
SSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01092. P5CS. 1 hit.
TIGR00407. proA. 1 hit.
TIGR01027. proB. 1 hit.
PROSITEiPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS01223. PROA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Isolation, characterization, and chromosomal location of a gene encoding the delta 1-pyrroline-5-carboxylate synthetase in Arabidopsis thaliana."
    Savoure A., Jaoua S., Hua X.J., Ardiles W., van Montagu M., Verbruggen N.
    FEBS Lett. 372:13-19(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: cv. Columbia.
  2. "Differential expression of two P5CS genes controlling proline accumulation during salt-stress requires ABA and is regulated by ABA1, ABI1 and AXR2 in Arabidopsis."
    Strizhov N., Abraham E., Oekresz L., Blickling S., Zilberstein A., Schell J., Koncz C., Szabados L.
    Plant J. 12:557-569(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  3. "Correlation between the induction of a gene for delta 1-pyrroline-5-carboxylate synthetase and the accumulation of proline in Arabidopsis thaliana under osmotic stress."
    Yoshiba Y., Kiyosue T., Katagiri T., Ueda H., Mizoguchi T., Yamaguchi-Shinozaki K., Wada K., Harada Y., Shinozaki K.
    Plant J. 7:751-760(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiP5CS1_ARATH
AccessioniPrimary (citable) accession number: P54887
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.