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O04015 (P5CS_ACTDE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Short name=P5CS

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
OrganismActinidia deliciosa (Kiwi)
Taxonomic identifier3627 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridsEricalesActinidiaceaeActinidia

Protein attributes

Sequence length717 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. HAMAP-Rule MF_00456

Catalytic activity

ATP + L-glutamate = ADP + L-glutamate 5-phosphate. HAMAP-Rule MF_00456

L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH. HAMAP-Rule MF_00456

Enzyme regulation

Feedback regulated by proline. HAMAP-Rule MF_00456

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. HAMAP-Rule MF_00456

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

Tissue specificity

Expressed at high levels in leaves and is inducible in roots subjected to salt stress.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 717717Delta-1-pyrroline-5-carboxylate synthase HAMAP-Rule MF_00456
PRO_0000109774

Regions

Nucleotide binding196 – 1972ATP By similarity
Nucleotide binding236 – 2427ATP By similarity
Region1 – 296296Glutamate 5-kinase HAMAP-Rule MF_00456
Region297 – 717421Gamma-glutamyl phosphate reductase HAMAP-Rule MF_00456

Sites

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

Sequences

Sequence LengthMass (Da)Tools
O04015 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: BC76103DB08C6F8C

FASTA71777,440
        10         20         30         40         50         60 
MDAVDSTRAF VKGVKRVIIK VGTAVVTRAD GRLALGRLGA LCEQIHELNS QGFEVILVTS 

        70         80         90        100        110        120 
GAVGVGRQRL RYRKLVNSSF ADLQKPQIEL DGKACAAVGQ NGLLALYDTL FSQLDVTSAQ 

       130        140        150        160        170        180 
LLVTDNDFRD PEFRKQLTET VESLLNLKVI PIFNENDAVS TRKAPYEDAS GIFWDNDSLA 

       190        200        210        220        230        240 
ALLALELKAD LLVLLSDVEG LYSGPPSDPQ SKLIHTYIKE MFEGLITFGD KSRVGRGGMT 

       250        260        270        280        290        300 
AKVKAAVYAA HAGIPVVITS GYATNNIIKV LQGERIGTLF HRDAQKWAPV GDVGARDMAV 

       310        320        330        340        350        360 
AARESSRRLQ AMSPQDRSKI LLDVADALEA NEKLIRIENE ADLAAAQQAG YEKSLISRLA 

       370        380        390        400        410        420 
LKSGKISSLA KSIRVLANME EPIGHVLKRT EITDGLVLEK TSSPLGVLLI IFESRPDALV 

       430        440        450        460        470        480 
QIASLAIRSG NGLVLKGGKE AKRSNAILHK VITSAIPENV GPRLIGLVTS REEIPDLLKL 

       490        500        510        520        530        540 
DDVIDLVIPR GSNKLVSQIK ESTKIPVLGH ADGICHVYVD KSANMDMAKK VVLDAKTDYP 

       550        560        570        580        590        600 
AACNAMETLL VHKDLVQNGC LDELIVELQI KGVVIHGGPR ASSLLHIPEA RSLHHEYSSL 

       610        620        630        640        650        660 
ACTIEIVDDV YAAIDHIHRH GSAHTDSIIT EDHEVAEIFL RQVDSSSVLH NASTRFSDGA 

       670        680        690        700        710 
RFGLGAEVGI STSRIHARGP VGVEGLLTTR WIARGSGQVV DGDKGIVYTH KDLTSHA 

« Hide

References

[1]"Regulation of proline accumulation in kiwifruit buds with and without hydrogen cyanamide treatment."
Walton E.F., Podivinsky E., Wu R.-M., Reynolds P.H.S., Young L.W.
Physiol. Plantarum 102:171-178(1998)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Axillary bud.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U92286 mRNA. Translation: AAC14481.1.

3D structure databases

ProteinModelPortalO04015.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00098; UER00359.
UPA00098; UER00360.

Family and domain databases

Gene3D3.40.1160.10. 1 hit.
3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPMF_00456. ProB.
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 nameP5CS_ACTDE
AccessionPrimary (citable) accession number: O04015
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 1, 1997
Last modified: February 19, 2014
This is version 85 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