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Q5R4M8 (P5CS_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 65. 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
Alternative name(s):
Aldehyde dehydrogenase family 18 member A1

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:ALDH18A1
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length795 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Bifunctional enzyme that converts glutamate to glutamate 5-semialdehyde, an intermediate in the biosynthesis of proline, ornithine and arginine By similarity.

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.

Subcellular location

Mitochondrion inner membrane By similarity.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 795795Delta-1-pyrroline-5-carboxylate synthase
PRO_0000294073

Regions

Nucleotide binding266 – 2672ATP By similarity
Nucleotide binding305 – 3117ATP By similarity
Region1 – 361361Glutamate 5-kinase
Region362 – 795434Gamma-glutamyl phosphate reductase

Sites

Binding site1171Substrate By similarity
Binding site2231Substrate By similarity
Binding site2461Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue3111N6-succinyllysine By similarity
Modified residue3471N6-succinyllysine By similarity
Modified residue5501N6-succinyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R4M8 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 3ACAE0F726665CD9

FASTA79587,341
        10         20         30         40         50         60 
MLSQVYRYGF QPFNQHLLPW VQCTTISRSH CIQPSVIRHV RSWSNIPFIT VPLSRTHGKS 

        70         80         90        100        110        120 
FAHRSELKHA KRIVVKLGSA VVTRGDECGL ALGRLASIVE QVSVLQNQGR EMMLVTSGAV 

       130        140        150        160        170        180 
AFGKQRLRHE ILLSQSVRQA LHSGQNQLKE MAIPVLEARA CAAAGQSGLM ALYEAMFTQY 

       190        200        210        220        230        240 
SICAAQILVT NLDFHDEQKR RNLNGTLHEL LRMNIVPIVN TNDAVVPPAE PNSDLQGVNV 

       250        260        270        280        290        300 
ISVKDNDSLA ARLAVEMKTD LLIVLSDVEG LFDSPPGSDD AKLIDIFYPG DQQSVTFGTK 

       310        320        330        340        350        360 
SRVGMGGMEA KVKAALWALQ GGTSVVIANG THPKVSGHVI TDIVEGKKVG TFFSEVKPAG 

       370        380        390        400        410        420 
PTVEQQGEMA RSGGRMLATL EPEQRAEIIH HLADLLTDQR DEILLANKKD LEEAEGRLAP 

       430        440        450        460        470        480 
PLLKRLSLST SKLNSLAIGL RQIAASSQDS VGRVLRRTRI AKNLELEQVT VPIGVLLVIF 

       490        500        510        520        530        540 
ESRPDCLPQV AALAIASGNG LLLKGGKEAA HSNRILHLLT QEALSIHGVK EAVQLVNTRE 

       550        560        570        580        590        600 
EVEDLCRLDK MIDLIIPRGS SQLVRDIQKA AKGIPVMGHS EGICHMYVDS EASVDKVTRL 

       610        620        630        640        650        660 
VRDSKCEYPA ACNALETLLI HRDLLRTPLF DQIIDMLRVE QVKIHAGPKF ASYLTFSPSE 

       670        680        690        700        710        720 
VKSLRTEYGD LELCIEVVDN VQDAIDHIHK YGSSHTDVIV TENENTAEFF LQHVDSACVF 

       730        740        750        760        770        780 
WNASTRFSDG YRFGLGAEVG ISTSRIHARG PVGLEGLLTT KWLLRGKDHV VSDFSEHGSL 

       790 
KYLHENLPIP QRNTN 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR861217 mRNA. Translation: CAH93288.1.

3D structure databases

ProteinModelPortalQ5R4M8.
SMRQ5R4M8. Positions 362-794.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5R4M8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG007911.
InParanoidQ5R4M8.

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.
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.
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.
PROSITEPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameP5CS_PONAB
AccessionPrimary (citable) accession number: Q5R4M8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: December 21, 2004
Last modified: March 19, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways