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P54887 (P5CS1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Delta-1-pyrroline-5-carboxylate synthase A

Short name=P5CS A

Including the following 2 domains:

  1. Glutamate 5-kinase
    Short name=GK
    EC=2.7.2.11
    Alternative name(s):
    Gamma-glutamyl kinase
  2. Gamma-glutamyl phosphate reductase
    Short name=GPR
    EC=1.2.1.41
    Alternative name(s):
    Glutamate-5-semialdehyde dehydrogenase
    Glutamyl-gamma-semialdehyde dehydrogenase
Gene names
Name:P5CSA
Synonyms:P5CS1
Ordered Locus Names:At2g39800
ORF Names:T5I7.10
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length717 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

ATP + L-glutamate = ADP + L-glutamate 5-phosphate.

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

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2.

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.

Sequence similarities

In the N-terminal section; belongs to the glutamate 5-kinase family.

In the C-terminal section; belongs to the gamma-glutamyl phosphate reductase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis
   Coding sequence diversityAlternative splicing
   LigandATP-binding
NADP
Nucleotide-binding
   Molecular functionKinase
Oxidoreductase
Transferase
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processL-proline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

hyperosmotic salinity response

Inferred from mutant phenotype PubMed 17971042. Source: TAIR

pollen development

Inferred from mutant phenotype PubMed 23234543. Source: TAIR

proline biosynthetic process

Inferred from mutant phenotype PubMed 17971042PubMed 23234543. Source: TAIR

response to oxidative stress

Inferred from mutant phenotype PubMed 17971042. Source: TAIR

response to water deprivation

Inferred from genetic interaction PubMed 21791601. Source: TAIR

root development

Inferred from mutant phenotype PubMed 17971042. Source: TAIR

   Cellular_componentchloroplast

Inferred from direct assay PubMed 17971042. Source: TAIR

membrane

Inferred from direct assay PubMed 17432890. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

delta1-pyrroline-5-carboxylate synthetase activity

Inferred from sequence or structural similarity PubMed 10441499. Source: TAIR

glutamate 5-kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

glutamate-5-semialdehyde dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: P54887-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 717717Delta-1-pyrroline-5-carboxylate synthase A
PRO_0000109772

Regions

Nucleotide binding196 – 1972ATP By similarity
Nucleotide binding236 – 2427ATP By similarity
Region1 – 296296Glutamate 5-kinase
Region297 – 717421Gamma-glutamyl phosphate reductase

Sites

Binding site601Substrate By similarity
Binding site1571Substrate By similarity
Binding site1761Substrate; via amide nitrogen By similarity

Experimental info

Sequence conflict421C → F in BAA06864. Ref.3
Sequence conflict541E → K in BAA06864. Ref.3
Sequence conflict3811D → E in BAA06864. Ref.3
Sequence conflict4671L → F in BAA06864. Ref.3
Sequence conflict6761H → Y in BAA06864. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: DF2B296362351A78

FASTA71777,702
        10         20         30         40         50         60 
MEELDRSRAF ARDVKRIVVK VGTAVVTGKG GRLALGRLGA LCEQLAELNS DGFEVILVSS 

        70         80         90        100        110        120 
GAVGLGRQRL RYRQLVNSSF ADLQKPQTEL DGKACAGVGQ SSLMAYYETM FDQLDVTAAQ 

       130        140        150        160        170        180 
LLVNDSSFRD KDFRKQLNET VKSMLDLRVI PIFNENDAIS TRRAPYQDSS GIFWDNDSLA 

       190        200        210        220        230        240 
ALLALELKAD LLILLSDVEG LYTGPPSDPN SKLIHTFVKE KHQDEITFGD KSRLGRGGMT 

       250        260        270        280        290        300 
AKVKAAVNAA YAGIPVIITS GYSAENIDKV LRGLRVGTLF HQDARLWAPI TDSNARDMAV 

       310        320        330        340        350        360 
AARESSRKLQ ALSSEDRKKI LLDIADALEA NVTTIKAENE LDVASAQEAG LEESMVARLV 

       370        380        390        400        410        420 
MTPGKISSLA ASVRKLADME DPIGRVLKKT EVADGLVLEK TSSPLGVLLI VFESRPDALV 

       430        440        450        460        470        480 
QIASLAIRSG NGLLLKGGKE ARRSNAILHK VITDAIPETV GGKLIGLVTS REEIPDLLKL 

       490        500        510        520        530        540 
DDVIDLVIPR GSNKLVTQIK NTTKIPVLGH ADGICHVYVD KACDTDMAKR IVSDAKLDYP 

       550        560        570        580        590        600 
AACNAMETLL VHKDLEQNAV LNELIFALQS NGVTLYGGPR ASKILNIPEA RSFNHEYCAK 

       610        620        630        640        650        660 
ACTVEVVEDV YGAIDHIHRH GSAHTDCIVT EDHEVAELFL RQVDSAAVFH NASTRFSDGF 

       670        680        690        700        710 
RFGLGAEVGV STGRIHARGP VGVEGLLTTR WIMRGKGQVV DGDNGIVYTH QDIPIQA 

« Hide

References

« Hide 'large scale' references
[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]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS66637.
T50685.
RefSeqNP_001189714.1. NM_001202785.1.
NP_181510.1. NM_129539.2.
UniGeneAt.20482.

3D structure databases

ProteinModelPortalP54887.
SMRP54887. Positions 13-284, 302-715.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid3904. 6 interactions.
IntActP54887. 6 interactions.
STRING3702.AT2G39800.1-P.

Proteomic databases

PaxDbP54887.
PRIDEP54887.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G39800.1; AT2G39800.1; AT2G39800.
AT2G39800.4; AT2G39800.4; AT2G39800.
GeneID818566.
KEGGath:AT2G39800.

Organism-specific databases

TAIRAT2G39800.

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHOG000246357.
InParanoidP54887.
KOK12657.
OMAFEARPDC.
PhylomeDBP54887.
ProtClustDBPLN02418.

Enzyme and pathway databases

BioCycARA:AT2G39800-MONOMER.
ARA:GQT-2788-MONOMER.
ARA:GQT-2789-MONOMER.
ARA:GQT-2790-MONOMER.
MetaCyc:AT2G39800-MONOMER.
UniPathwayUPA00098; UER00359.
UPA00098; UER00360.

Gene expression databases

ArrayExpressP54887.
GenevestigatorP54887.

Family and domain databases

Gene3D3.40.1160.10. 1 hit.
3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR000965. G-glutamylP_reductase.
IPR020593. G-glutamylP_reductase_CS.
IPR001057. Glu/AcGlu_kinase.
IPR005715. Glu_5kinase/COase_Synthase.
IPR019797. Glutamate_5-kinase_CS.
IPR005766. P5_carboxy_syn.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
PF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF036429. P5C_syn. 1 hit.
PRINTSPR00474. GLU5KINASE.
SUPFAMSSF53633. SSF53633. 1 hit.
SSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR01092. P5CS. 1 hit.
TIGR00407. proA. 1 hit.
TIGR01027. proB. 1 hit.
PROSITEPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameP5CS1_ARATH
AccessionPrimary (citable) accession number: P54887
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 19, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names