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P54888 (P5CS2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. 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 B

Short name=P5CS B

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:P5CSB
Synonyms:P5CS2
Ordered Locus Names:At3g55610
ORF Names:F1I16_20
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length726 AA.
Sequence statusComplete.
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.

Sequence caution

The sequence CAB81586.1 differs from that shown. Reason: Erroneous gene model prediction.

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: P54888-1)

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 – 726726Delta-1-pyrroline-5-carboxylate synthase B
PRO_0000109773

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

Sequences

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

Last modified October 1, 1996. Version 1.
Checksum: E01446A6659021FF

FASTA72678,871
        10         20         30         40         50         60 
MTEIDRSRAF AKDVKRIVVK VGTAVVTGKG GRLALGRLGA ICEQLAELNS DGFEVILVSS 

        70         80         90        100        110        120 
GAVGLGRQRL RYRQLVNSSF ADLQKPQMEL DGKACAGVGQ SSLMAYYETM FDQLDVTVAQ 

       130        140        150        160        170        180 
MLVTDSSFRD KDFRKQLSET VKAMLRMRVI PVFNENDAIS TRRAPYKDST GIFWDNDSLA 

       190        200        210        220        230        240 
ALLSLELKAD LLILLSDVEG LYTGPPSDST SKLIHTFIKE KHQDEITFGE KSKLGRGGMT 

       250        260        270        280        290        300 
AKVKAAVNAA YGGVPVIITS GYAAENISKV LRGLRVGTLF HQDAHLWAPV VDTTSRDMAV 

       310        320        330        340        350        360 
AARESSRKLQ ALSSEDRKQI LHDIANALEV NEKTIKAEND LDVAAAQEAG YEESLVARLV 

       370        380        390        400        410        420 
MKPGKISSLA ASVRQLAEME DPIGRVLKKT QVADDLILEK TSSPIGVLLI VFESRPDALV 

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

       490        500        510        520        530        540 
DDVIDLVIPR GSNKLVSQIK NSTKIPVLGH ADGICHVYVD KSGKLDMAKR IVSDAKLDYP 

       550        560        570        580        590        600 
AACNAMETLL VHKDLEQNGF LDDLIYVLQT KGVTLYGGPR ASAKLNIPET KSFHHEYSSK 

       610        620        630        640        650        660 
ACTVEIVEDV YGAIDHIHQH GSAHTDCIVT EDSEVAEIFL RQVDSAAVFH NASTRFSDGF 

       670        680        690        700        710        720 
RFGLGAEVGI STSRIHARGP VGVEGLLTTR WIMRGKGQVV DGDNGIVYTH KDLPVLQRTE 


AVENGI 

« Hide

References

« Hide 'large scale' references
[1]"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 [GENOMIC DNA / MRNA].
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X86778 Genomic DNA. Translation: CAA60447.1.
Y09355 mRNA. Translation: CAA70527.1.
AL161667 Genomic DNA. Translation: CAB81586.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE79408.1.
AY091766 mRNA. Translation: AAM10314.1.
PIRT47700.
T50684. T50682.
RefSeqNP_191120.2. NM_115419.4.
UniGeneAt.25196.

3D structure databases

ProteinModelPortalP54888.
SMRP54888. Positions 13-284, 294-719.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid10043. 2 interactions.
IntActP54888. 2 interactions.

Proteomic databases

PaxDbP54888.
PRIDEP54888.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G55610.1; AT3G55610.1; AT3G55610. [P54888-1]
GeneID824727.
KEGGath:AT3G55610.

Organism-specific databases

TAIRAT3G55610.

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHOG000246357.
InParanoidP54888.
KOK12657.
OMALLPWVQS.
PhylomeDBP54888.
ProtClustDBPLN02418.

Enzyme and pathway databases

BioCycARA:GQT-931-MONOMER.
UniPathwayUPA00098; UER00359.
UPA00098; UER00360.

Gene expression databases

GenevestigatorP54888.

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.
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.
[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 nameP5CS2_ARATH
AccessionPrimary (citable) accession number: P54888
Secondary accession number(s): Q9M061
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 117 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