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O65361 (P5CS_MESCR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. 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
Gene names
Name:P5CS
OrganismMesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum)
Taxonomic identifier3544 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAizoaceaeMesembryanthemum

Protein attributes

Sequence length719 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 – 719719Delta-1-pyrroline-5-carboxylate synthase HAMAP-Rule MF_00456
PRO_0000109776

Regions

Nucleotide binding193 – 1942ATP By similarity
Nucleotide binding233 – 2397ATP By similarity
Region1 – 293293Glutamate 5-kinase HAMAP-Rule MF_00456
Region294 – 719426Gamma-glutamyl phosphate reductase HAMAP-Rule MF_00456

Sites

Binding site571Substrate By similarity
Binding site1541Substrate By similarity
Binding site1731Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
O65361 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 1510D11AF5559961

FASTA71977,855
        10         20         30         40         50         60 
MDATRAFVKD VKRVVVKVGT AVVTRSDGRL ALGRLGSLCE QLKELNSDGY EVILVTSGAV 

        70         80         90        100        110        120 
SAGRQRLRFR KLVNSSFADL QKPQVELDGK ACAAVGQNGL MALYDTLFSQ LDLTAAQLLV 

       130        140        150        160        170        180 
TDNDFRDPSF RTQLTETVYQ LLDLKVVPVL NENDAVSTRK APYEDSSGIF WDNDSLAALL 

       190        200        210        220        230        240 
ALELKADLLI LLSDVDGLYN GPPSDPRSKL ISTYVKEKHQ GEITFGDKSR LGRGGMTAKV 

       250        260        270        280        290        300 
KAAVYAAYAG IPVIIASGKA TDNIIKVIDG QCVGTLFHKD AHLWVQVKET GVRDMAVAAR 

       310        320        330        340        350        360 
ESSRRLQAVS SEERKKILLD IADALEANEE KILAENEADV AAAQYAGYDR SLVARLAMNP 

       370        380        390        400        410        420 
DKISSLAKSI RVLADMEEPI GRILKRTEIA DGLILEKTSC PLGVLLIVFE SRPDALVQIA 

       430        440        450        460        470        480 
SLAIRSGNGL LLKGGKEAKR SNAILHKVIT SAIPDKVGEK LIGLVTSRDE IPDLLKLDDV 

       490        500        510        520        530        540 
IDLVIPRGSN KLVSQIKEST RIPVLGHADG ICHVYVDKSA NMDMAKRIVL DAKTDYPAAC 

       550        560        570        580        590        600 
NAMETLLVHK DLAENGGLND LIVDLRTEGV TMFGGPRIDA LQEFNIQATQ TFNREYSSPA 

       610        620        630        640        650        660 
CTVEIVDDVY AAIEHINHHG SAHTDCIIAE DHKVAETFLQ LVDSAAVLHN ASTRFCDGFR 

       670        680        690        700        710 
FGLGAEVGIS TSRIHARGPV GVEGLLTTRW VLKGSGQVVH GDKGVVYTHK DLPLVAQNS 

« Hide

References

[1]"Mesembryanthemum crystallinum pyrroline-5-carboxylate synthetase mRNA."
Michalowski C.B., Quigley-Landreau F., Bohnert H.J.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF067967 mRNA. Translation: AAC18862.1.
PIRT12258.

3D structure databases

ProteinModelPortalO65361.
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_MESCR
AccessionPrimary (citable) accession number: O65361
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: February 19, 2014
This is version 83 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