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Reviewed, UniProtKB/Swiss-Prot P54887 (P5CS1_ARATH)

Last modified November 25, 2008. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Delta-1-pyrroline-5-carboxylate synthetase A
      Short name=P5CS A
Including the following 2 domains:
    1- Recommended name:
            Glutamate 5-kinase
                Short name=GK
              EC=2.7.2.11
        Alternative name(s):
            Gamma-glutamyl kinase
    2- Recommended name:
            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) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length717 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript 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

Alternative products

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

Notes: 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 synthetase A
PRO_0000109772

Regions

Region1 – 296296Glutamate 5-kinase
Region297 – 717421Gamma-glutamyl phosphate reductase

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: 7556633] [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: 9351242] [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: 7773306] [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: 10617197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[5]"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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.

Cross-references

Sequence databases

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.
AF424633 mRNA. Translation: AAL11626.1.
AY113046 mRNA. Translation: AAM47354.1.
AY150430 mRNA. Translation: AAN12972.1.
PIRS66637.
T50685.
RefSeqNP_181510.1.
UniGeneAt.20482

3D structure databases

HSSPHSSP built from PDB template 1O20 based on UniProtKB Q9WYC9.
ModBaseSearch...

Genome annotation databases

GeneID818566.
GenomeReviewsGene locus AT2G39800 in contig CT485783_GR.
KEGGath:AT2G39800.

Organism-specific databases

TAIRAt2g39800.

Gene expression databases

GermOnlineAT2G39800. Arabidopsis thaliana.

Family and domain databases

InterProIPR016163. Ald_DHase_C.
IPR016162. Ald_DHase_N.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR000965. Gglut_pp_reduct.
IPR001057. Glu_5kinase.
IPR005766. P5_carboxy_syn.
IPR005715. ProB.
[Graphical view]
Gene3DG3DSA:3.40.1160.10. Aa_kinase. 1 hit.
G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PfamPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFPIRSF036429. P5C_syn. 1 hit.
PRINTSPR00474. GLU5KINASE.
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: November 25, 2008
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents