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Q9Z110

- P5CS_MOUSE

UniProt

Q9Z110 - P5CS_MOUSE

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
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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

    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

    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

    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-SubCell
    2. mitochondrion Source: MGI

    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

    ArrayExpressiQ9Z110.
    BgeeiQ9Z110.
    CleanExiMM_ALDH18A1.
    GenevestigatoriQ9Z110.

    Interactioni

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z110.
    SMRiQ9Z110. Positions 70-353, 362-793.
    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.
    InParanoidiQ8BGM2.
    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

    MLRHMHRSGV QPFRQRLLPW VQSIAVPRSN RVQPSAIRHV RSWSNIPFIT    50
    VPLSRAHGKP FAHRSELKHA KRIVVKLGSA VVTRGDECGL ALGRLASIVE 100
    QVSVLQNQGR EMMLVTSGAV AFGKQRLRHE ILLSQSVRQA LHSGQNHLKE 150
    MAIPVLEARA CAAAGQSGLM ALYEAMFTQY SICAAQILVT NLDFHDEQKR 200
    RNLNGTLHEL LRMNIVPIVN TNDAVVPPAE PNSDLQGVNV ISVKDNDSLA 250
    ARLAVEMKTD LLIVLSDVEG LFDSPPGSDD AKLIDIFYPG DQQSVTFGTK 300
    SRVGLGGMEA KVKAALWALQ GGTSVVIANG THPKVSGHVI TDIVEGKKVG 350
    TFFSEVKPAG PTVEQQGEMA RSGGRMLATL EPEQRAEIIN HLADLLTDQR 400
    EEILLANKKD LEEAEGRLAS PLLKRLSLST SKLNSLAIGL RQIAASSQES 450
    VGRVLRRTRI AKNLELEQVT VPIGVLLVIF ESRPDCLPQV AALAIASGNG 500
    LLLKGGKEAA HSNRILHLLT QEALSIHGVK EAIQLVNTRE EVEDLCRLDK 550
    IIDLIIPRGS SQLVRDIQKA AKGIPVMGHS EGICHMYVDS EASVDKVTRL 600
    VRDSKCEYPA ACNALETLLI HRDLLRTPLF DQIIDMLRVE QVKIHAGPKF 650
    ASYLTFSPSE VKSLRTEYGD LEVCIEVVDS VQEAIDHIHK YGSSHTDVIV 700
    TENEKTAEFF LQHVDSACVF WNASTRFSDG YRFGLGAEVG ISTSRIHARG 750
    PVGLEGLLTT KWLLRGQDHV VSDFSEHGSL KYLHENLPVP QRNFS 795
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 70-353, 362-793.
    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 Q8BGM2.
    KOi K12657.
    OMAi LLPWVQS.
    OrthoDBi EOG7WX07N.
    TreeFami TF314372.

    Enzyme and pathway databases

    UniPathwayi UPA00098 ; UER00359 .
    UPA00098 ; UER00360 .

    Miscellaneous databases

    ChiTaRSi ALDH18A1. mouse.
    NextBioi 312680.
    PROi Q9Z110.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z110.
    Bgeei Q9Z110.
    CleanExi MM_ALDH18A1.
    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

    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: October 1, 2014
    This is version 135 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