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Q9Z110 (P5CS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. 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

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
Synonyms:P5cs, Pycs
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length795 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

Enzyme regulation

The short isoform isinhibited by L-ornithine with a Ki of approximately 0.25 mm. The long isoform isinsensitive to ornithine inhibition. Thus, the two amino acid insert in the long isoform abolishesfeedback inhibition of P5CS activity by L-ornithine. Ref.1

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.

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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q9Z110-1)

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.
Isoform Short (identifier: Q9Z110-2)

The sequence of this isoform differs from the canonical sequence as follows:
     239-240: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 795795Delta-1-pyrroline-5-carboxylate synthase
PRO_0000109770

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 Ref.5
Modified residue3471N6-succinyllysine Ref.5
Modified residue5501N6-succinyllysine Ref.5

Natural variations

Alternative sequence239 – 2402Missing in isoform Short.
VSP_005216

Experimental info

Sequence conflict5821G → S in AAD17517. Ref.1
Sequence conflict5821G → S in AAD17518. Ref.1

Sequences

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

Last modified July 27, 2011. Version 2.
Checksum: 877DF1A7B5F84247

FASTA79587,266
        10         20         30         40         50         60 
MLRHMHRSGV QPFRQRLLPW VQSIAVPRSN RVQPSAIRHV RSWSNIPFIT VPLSRAHGKP 

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

       130        140        150        160        170        180 
AFGKQRLRHE ILLSQSVRQA LHSGQNHLKE 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 
SRVGLGGMEA KVKAALWALQ GGTSVVIANG THPKVSGHVI TDIVEGKKVG TFFSEVKPAG 

       370        380        390        400        410        420 
PTVEQQGEMA RSGGRMLATL EPEQRAEIIN HLADLLTDQR EEILLANKKD LEEAEGRLAS 

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

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

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

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

       670        680        690        700        710        720 
VKSLRTEYGD LEVCIEVVDS VQEAIDHIHK YGSSHTDVIV TENEKTAEFF LQHVDSACVF 

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

       790 
KYLHENLPVP QRNFS 

« Hide

Isoform Short [UniParc].

Checksum: F0076527C19FCDCD
Show »

FASTA79387,053

References

« Hide 'large scale' references
[1]"Molecular enzymology of mammalian delta1-pyrroline-5-carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition."
Hu C.A., Lin W.-W., Obie C., Valle D.
J. Biol. Chem. 274:6754-6762(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, ENZYME REGULATION.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Bone marrow, Kidney and Thymus.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N and FVB/N-3.
Tissue: Mammary tumor and Salivary gland.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-311; LYS-347 AND LYS-550, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF056573 mRNA. Translation: AAD17517.1.
AF056574 mRNA. Translation: AAD17518.1.
AK151072 mRNA. Translation: BAE30088.1.
AK153946 mRNA. Translation: BAE32270.1.
AK168905 mRNA. Translation: BAE40719.1.
CH466534 Genomic DNA. Translation: EDL41837.1.
BC033427 mRNA. Translation: AAH33427.1.
BC037699 mRNA. Translation: AAH37699.1.
RefSeqNP_062672.2. NM_019698.2.
NP_705782.2. NM_153554.2.
XP_006527292.1. XM_006527229.1.
UniGeneMm.233117.

3D structure databases

ProteinModelPortalQ9Z110.
SMRQ9Z110. Positions 70-353, 362-793.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9Z110. 1 interaction.
MINTMINT-4998531.
STRING10090.ENSMUSP00000025979.

PTM databases

PhosphoSiteQ9Z110.

Proteomic databases

PaxDbQ9Z110.
PRIDEQ9Z110.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025979; ENSMUSP00000025979; ENSMUSG00000025007. [Q9Z110-1]
ENSMUST00000176939; ENSMUSP00000135426; ENSMUSG00000025007. [Q9Z110-2]
GeneID56454.
KEGGmmu:56454.
UCSCuc008hkw.2. mouse. [Q9Z110-2]
uc008hkx.2. mouse. [Q9Z110-1]

Organism-specific databases

CTD5832.
MGIMGI:1888908. Aldh18a1.

Phylogenomic databases

eggNOGCOG0014.
GeneTreeENSGT00500000044903.
HOGENOMHOG000246357.
HOVERGENHBG007911.
InParanoidQ8BGM2.
KOK12657.
OMALLPWVQS.
OrthoDBEOG7WX07N.
TreeFamTF314372.

Enzyme and pathway databases

UniPathwayUPA00098; UER00359.
UPA00098; UER00360.

Gene expression databases

ArrayExpressQ9Z110.
BgeeQ9Z110.
CleanExMM_ALDH18A1.
GenevestigatorQ9Z110.

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...

Other

ChiTaRSALDH18A1. mouse.
NextBio312680.
PROQ9Z110.
SOURCESearch...

Entry information

Entry nameP5CS_MOUSE
AccessionPrimary (citable) accession number: Q9Z110
Secondary accession number(s): Q8BGM2, Q9R1P6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 130 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot