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Q9Z110

- P5CS_MOUSE

UniProt

Q9Z110 - P5CS_MOUSE

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Protein

Delta-1-pyrroline-5-carboxylate synthase

Gene

Aldh18a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

ATP + L-glutamate = ADP + L-glutamate 5-phosphate.
L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH.

Enzyme regulationi

The short isoform is inhibited by L-ornithine with a Ki of approximately 0.25 mm. The long isoform is insensitive to ornithine inhibition. Thus, the two amino acid insert in the long isoform abolishes feedback inhibition of P5CS activity by L-ornithine.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei117 – 1171SubstrateBy similarity
Binding sitei223 – 2231SubstrateBy similarity
Binding sitei246 – 2461Substrate; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi266 – 2672ATPBy similarity
Nucleotide bindingi305 – 3117ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate 5-kinase activity Source: MGI
  3. glutamate-5-semialdehyde dehydrogenase activity Source: UniProtKB
  4. poly(A) RNA binding Source: Ensembl

GO - Biological processi

  1. cellular amino acid biosynthetic process Source: MGI
  2. citrulline biosynthetic process Source: UniProtKB
  3. glutamate metabolic process Source: UniProtKB
  4. L-proline biosynthetic process Source: UniProtKB-UniPathway
  5. ornithine biosynthetic process Source: Ensembl
  6. proline biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Oxidoreductase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Proline biosynthesis

Keywords - Ligandi

ATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_239550. Amino acid synthesis and interconversion (transamination).
UniPathwayiUPA00098; UER00359.
UPA00098; UER00360.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-1-pyrroline-5-carboxylate synthase
Short name:
P5CS
Alternative name(s):
Aldehyde dehydrogenase family 18 member A1
Including the following 2 domains:
Glutamate 5-kinase (EC:2.7.2.11)
Short name:
GK
Alternative name(s):
Gamma-glutamyl kinase
Gamma-glutamyl phosphate reductase (EC:1.2.1.41)
Short name:
GPR
Alternative name(s):
Glutamate-5-semialdehyde dehydrogenase
Glutamyl-gamma-semialdehyde dehydrogenase
Gene namesi
Name:Aldh18a1
Synonyms:P5cs, Pycs
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:1888908. Aldh18a1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB-KW
  2. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 795795Delta-1-pyrroline-5-carboxylate synthasePRO_0000109770Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei311 – 3111N6-succinyllysine1 Publication
Modified residuei347 – 3471N6-succinyllysine1 Publication
Modified residuei550 – 5501N6-succinyllysine1 Publication

Proteomic databases

MaxQBiQ9Z110.
PaxDbiQ9Z110.
PRIDEiQ9Z110.

PTM databases

PhosphoSiteiQ9Z110.

Expressioni

Gene expression databases

BgeeiQ9Z110.
CleanExiMM_ALDH18A1.
ExpressionAtlasiQ9Z110. baseline and differential.
GenevestigatoriQ9Z110.

Interactioni

Protein-protein interaction databases

BioGridi207993. 1 interaction.
IntActiQ9Z110. 1 interaction.
MINTiMINT-4998531.
STRINGi10090.ENSMUSP00000025979.

Structurei

3D structure databases

ProteinModelPortaliQ9Z110.
SMRiQ9Z110. Positions 60-793.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 361361Glutamate 5-kinaseAdd
BLAST
Regioni362 – 795434Gamma-glutamyl phosphate reductaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the glutamate 5-kinase family.Curated
In the C-terminal section; belongs to the gamma-glutamyl phosphate reductase family.Curated

Phylogenomic databases

eggNOGiCOG0014.
GeneTreeiENSGT00500000044903.
HOGENOMiHOG000246357.
HOVERGENiHBG007911.
InParanoidiQ9Z110.
KOiK12657.
OMAiLLPWVQS.
OrthoDBiEOG7WX07N.
TreeFamiTF314372.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPiMF_00412. ProA.
MF_00456. ProB.
InterProiIPR016161. 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]
PfamiPF00696. AA_kinase. 1 hit.
PF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFiPIRSF036429. P5C_syn. 1 hit.
PRINTSiPR00474. GLU5KINASE.
SUPFAMiSSF53633. SSF53633. 1 hit.
SSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01092. P5CS. 1 hit.
TIGR00407. proA. 1 hit.
PROSITEiPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS01223. PROA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: Q9Z110-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MLRHMHRSGV QPFRQRLLPW VQSIAVPRSN RVQPSAIRHV RSWSNIPFIT
60 70 80 90 100
VPLSRAHGKP FAHRSELKHA KRIVVKLGSA VVTRGDECGL ALGRLASIVE
110 120 130 140 150
QVSVLQNQGR EMMLVTSGAV AFGKQRLRHE ILLSQSVRQA LHSGQNHLKE
160 170 180 190 200
MAIPVLEARA CAAAGQSGLM ALYEAMFTQY SICAAQILVT NLDFHDEQKR
210 220 230 240 250
RNLNGTLHEL LRMNIVPIVN TNDAVVPPAE PNSDLQGVNV ISVKDNDSLA
260 270 280 290 300
ARLAVEMKTD LLIVLSDVEG LFDSPPGSDD AKLIDIFYPG DQQSVTFGTK
310 320 330 340 350
SRVGLGGMEA KVKAALWALQ GGTSVVIANG THPKVSGHVI TDIVEGKKVG
360 370 380 390 400
TFFSEVKPAG PTVEQQGEMA RSGGRMLATL EPEQRAEIIN HLADLLTDQR
410 420 430 440 450
EEILLANKKD LEEAEGRLAS PLLKRLSLST SKLNSLAIGL RQIAASSQES
460 470 480 490 500
VGRVLRRTRI AKNLELEQVT VPIGVLLVIF ESRPDCLPQV AALAIASGNG
510 520 530 540 550
LLLKGGKEAA HSNRILHLLT QEALSIHGVK EAIQLVNTRE EVEDLCRLDK
560 570 580 590 600
IIDLIIPRGS SQLVRDIQKA AKGIPVMGHS EGICHMYVDS EASVDKVTRL
610 620 630 640 650
VRDSKCEYPA ACNALETLLI HRDLLRTPLF DQIIDMLRVE QVKIHAGPKF
660 670 680 690 700
ASYLTFSPSE VKSLRTEYGD LEVCIEVVDS VQEAIDHIHK YGSSHTDVIV
710 720 730 740 750
TENEKTAEFF LQHVDSACVF WNASTRFSDG YRFGLGAEVG ISTSRIHARG
760 770 780 790
PVGLEGLLTT KWLLRGQDHV VSDFSEHGSL KYLHENLPVP QRNFS
Length:795
Mass (Da):87,266
Last modified:July 27, 2011 - v2
Checksum:i877DF1A7B5F84247
GO
Isoform Short (identifier: Q9Z110-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:793
Mass (Da):87,053
Checksum:iF0076527C19FCDCD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti582 – 5821G → S in AAD17517. (PubMed:10037775)Curated
Sequence conflicti582 – 5821G → S in AAD17518. (PubMed:10037775)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei239 – 2402Missing in isoform Short. CuratedVSP_005216

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29803.1. [Q9Z110-1]
CCDS57144.1. [Q9Z110-2]
RefSeqiNP_062672.2. NM_019698.2. [Q9Z110-1]
NP_705782.2. NM_153554.2. [Q9Z110-2]
XP_006527292.1. XM_006527229.1. [Q9Z110-1]
UniGeneiMm.233117.

Genome annotation databases

EnsembliENSMUST00000025979; ENSMUSP00000025979; ENSMUSG00000025007. [Q9Z110-1]
ENSMUST00000176939; ENSMUSP00000135426; ENSMUSG00000025007. [Q9Z110-2]
GeneIDi56454.
KEGGimmu:56454.
UCSCiuc008hkw.2. mouse. [Q9Z110-2]
uc008hkx.2. mouse. [Q9Z110-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS29803.1. [Q9Z110-1 ]
CCDS57144.1. [Q9Z110-2 ]
RefSeqi NP_062672.2. NM_019698.2. [Q9Z110-1 ]
NP_705782.2. NM_153554.2. [Q9Z110-2 ]
XP_006527292.1. XM_006527229.1. [Q9Z110-1 ]
UniGenei Mm.233117.

3D structure databases

ProteinModelPortali Q9Z110.
SMRi Q9Z110. Positions 60-793.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 207993. 1 interaction.
IntActi Q9Z110. 1 interaction.
MINTi MINT-4998531.
STRINGi 10090.ENSMUSP00000025979.

PTM databases

PhosphoSitei Q9Z110.

Proteomic databases

MaxQBi Q9Z110.
PaxDbi Q9Z110.
PRIDEi Q9Z110.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025979 ; ENSMUSP00000025979 ; ENSMUSG00000025007 . [Q9Z110-1 ]
ENSMUST00000176939 ; ENSMUSP00000135426 ; ENSMUSG00000025007 . [Q9Z110-2 ]
GeneIDi 56454.
KEGGi mmu:56454.
UCSCi uc008hkw.2. mouse. [Q9Z110-2 ]
uc008hkx.2. mouse. [Q9Z110-1 ]

Organism-specific databases

CTDi 5832.
MGIi MGI:1888908. Aldh18a1.

Phylogenomic databases

eggNOGi COG0014.
GeneTreei ENSGT00500000044903.
HOGENOMi HOG000246357.
HOVERGENi HBG007911.
InParanoidi Q9Z110.
KOi K12657.
OMAi LLPWVQS.
OrthoDBi EOG7WX07N.
TreeFami TF314372.

Enzyme and pathway databases

UniPathwayi UPA00098 ; UER00359 .
UPA00098 ; UER00360 .
Reactomei REACT_239550. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

ChiTaRSi Aldh18a1. mouse.
NextBioi 312680.
PROi Q9Z110.
SOURCEi Search...

Gene expression databases

Bgeei Q9Z110.
CleanExi MM_ALDH18A1.
ExpressionAtlasi Q9Z110. baseline and differential.
Genevestigatori Q9Z110.

Family and domain databases

Gene3Di 3.40.1160.10. 1 hit.
3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPi MF_00412. ProA.
MF_00456. ProB.
InterProi IPR016161. 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 ]
Pfami PF00696. AA_kinase. 1 hit.
PF00171. Aldedh. 1 hit.
[Graphical view ]
PIRSFi PIRSF036429. P5C_syn. 1 hit.
PRINTSi PR00474. GLU5KINASE.
SUPFAMi SSF53633. SSF53633. 1 hit.
SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR01092. P5CS. 1 hit.
TIGR00407. proA. 1 hit.
PROSITEi PS00902. GLUTAMATE_5_KINASE. 1 hit.
PS01223. PROA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiP5CS_MOUSE
AccessioniPrimary (citable) accession number: Q9Z110
Secondary accession number(s): Q8BGM2, Q9R1P6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3