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Q3THK7

- GUAA_MOUSE

UniProt

Q3THK7 - GUAA_MOUSE

Protein

GMP synthase [glutamine-hydrolyzing]

Gene

Gmps

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (17 Apr 2007)
      Previous versions | rss
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    Functioni

    Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division.By similarity

    Catalytic activityi

    ATP + XMP + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei104 – 1041For GATase activityPROSITE-ProRule annotation
    Active sitei190 – 1901For GATase activityPROSITE-ProRule annotation
    Active sitei192 – 1921For GATase activityPROSITE-ProRule annotation
    Binding sitei337 – 3371SubstrateBy similarity
    Binding sitei522 – 5221SubstrateBy similarity
    Binding sitei610 – 6101SubstrateBy similarity
    Binding sitei685 – 6851SubstrateBy similarity
    Binding sitei691 – 6911SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi244 – 2507ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. GMP synthase (glutamine-hydrolyzing) activity Source: UniProtKB-EC
    3. pyrophosphatase activity Source: InterPro

    GO - Biological processi

    1. glutamine metabolic process Source: UniProtKB-KW
    2. GMP biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    GMP biosynthesis, Purine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00189; UER00296.

    Protein family/group databases

    MEROPSiC26.950.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GMP synthase [glutamine-hydrolyzing] (EC:6.3.5.2)
    Alternative name(s):
    GMP synthetase
    Glutamine amidotransferase
    Gene namesi
    Name:Gmps
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:2448526. Gmps.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 693692GMP synthase [glutamine-hydrolyzing]PRO_0000284365Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei9 – 91N6-acetyllysineBy similarity
    Modified residuei318 – 3181PhosphothreonineBy similarity
    Modified residuei332 – 3321PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ3THK7.
    PaxDbiQ3THK7.
    PRIDEiQ3THK7.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00351252.

    PTM databases

    PhosphoSiteiQ3THK7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ3THK7.
    BgeeiQ3THK7.
    CleanExiMM_GMPS.
    GenevestigatoriQ3THK7.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi230837. 2 interactions.
    STRINGi10090.ENSMUSP00000029405.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3THK7.
    SMRiQ3THK7. Positions 23-693.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 216190Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd
    BLAST
    Domaini217 – 435219GMPS ATP-PPasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 glutamine amidotransferase type-1 domain.PROSITE-ProRule annotation
    Contains 1 GMPS ATP-PPase (ATP pyrophosphatase) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiCOG0519.
    GeneTreeiENSGT00390000006591.
    HOGENOMiHOG000223965.
    HOVERGENiHBG005929.
    InParanoidiQ3THK7.
    KOiK01951.
    OMAiGTVHKKN.
    OrthoDBiEOG7J17Z9.
    PhylomeDBiQ3THK7.
    TreeFamiTF106132.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    3.40.50.880. 1 hit.
    InterProiIPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR001674. GMP_synth_C.
    IPR004739. GMP_synth_N.
    IPR025777. GMPS_ATP_PPase_dom.
    IPR022310. NAD/GMP_synthase.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PfamiPF00117. GATase. 1 hit.
    PF00958. GMP_synt_C. 1 hit.
    PF02540. NAD_synthase. 1 hit.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.
    TIGRFAMsiTIGR00888. guaA_Nterm. 1 hit.
    PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
    PS51553. GMPS_ATP_PPASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q3THK7-1 [UniParc]FASTAAdd to Basket

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    MALCNGDSKP ENAGGDLKDG SHHYEGAVVI LDAGAQYGKV IDRRVRELFV    50
    QSEIFPLETP AFAIKEQGFR AIIISGGPNS VYAEDAPWFD PAIFTIGKPI 100
    LGICYGMQMM NKVFGGTVHK KSVREDGVFN ISMDNTCSLF RGLQKEEIVL 150
    LTHGDSVDKV ADGFKVVARS GNIVAGIANE SKKLYGVQFH PEVGLTENGK 200
    VILKNFLYDI AGCSGNFTVQ NRELECIREI KEKVGTSKVL VLLSGGVDST 250
    VCTALLNRAL NQDQVIAVHI DNGFMRKRES QSVEEALKKL GIQVKVINAA 300
    HSFYNGTTTL PISDEDRTPR KRISKTLNMT TSPEEKRKII GDTFVKIANE 350
    VIGEMSLKPE EVFLAQGTLR PDLIESASLV ASGKAELIKT HHNDTELIRK 400
    LREEGKVIEP LKDFHKDEVR ILGRELDLPE ELVSRHPFPG PGLAIRVICA 450
    EEPYICKDFP ETNNILKIVA DFSASVKKPH TLLQRVKACT TEEDQEKLMQ 500
    ITSLHSLNAF LLPIKTVGVQ GDCRSYSYVC GISSKDEPDW ESLIFLARLI 550
    PRMCHNINRV VYIFGPPVKE PPTDVTPTFL TTGVLSTLRQ ADFEAHNILR 600
    ESGFAGKISQ MPVILTPLHF DRDPLQKQPS CQRSVVIRTF ITSDFMTGVP 650
    ATPGNEIPVE VVLKMVTEIK KIPGISRIMY DLTSKPPGTT EWE 693
    Length:693
    Mass (Da):76,723
    Last modified:April 17, 2007 - v2
    Checksum:i854DBAD6A9C75A12
    GO

    Sequence cautioni

    The sequence BAE20667.1 differs from that shown. Reason: Frameshift at position 35.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti201 – 2011V → I in BAE39875. (PubMed:16141072)Curated
    Sequence conflicti205 – 2051N → Y in BAE39875. (PubMed:16141072)Curated
    Sequence conflicti265 – 2651V → D in BAE39875. (PubMed:16141072)Curated
    Sequence conflicti356 – 3561S → G in BAE40189. (PubMed:16141072)Curated
    Sequence conflicti359 – 3591P → H in BAE40189. (PubMed:16141072)Curated
    Sequence conflicti359 – 3591P → R in BAE39875. (PubMed:16141072)Curated
    Sequence conflicti363 – 3631Missing in BAE39875. (PubMed:16141072)Curated
    Sequence conflicti511 – 5122LL → CC in BAE27334. (PubMed:16141072)Curated
    Sequence conflicti586 – 5861S → G in BAE39875. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK049755 mRNA. Translation: BAE20667.1. Frameshift.
    AK143197 mRNA. Translation: BAE25299.1.
    AK146654 mRNA. Translation: BAE27334.1.
    AK167857 mRNA. Translation: BAE39875.1.
    AK168239 mRNA. Translation: BAE40189.1.
    AK169043 mRNA. Translation: BAE40832.1.
    AK169701 mRNA. Translation: BAE41314.1.
    BC080685 mRNA. Translation: AAH80685.1.
    CCDSiCCDS17383.1.
    RefSeqiNP_001028472.2. NM_001033300.2.
    UniGeneiMm.331051.
    Mm.394565.
    Mm.490620.

    Genome annotation databases

    EnsembliENSMUST00000029405; ENSMUSP00000029405; ENSMUSG00000027823.
    GeneIDi229363.
    KEGGimmu:229363.
    UCSCiuc008pke.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK049755 mRNA. Translation: BAE20667.1 . Frameshift.
    AK143197 mRNA. Translation: BAE25299.1 .
    AK146654 mRNA. Translation: BAE27334.1 .
    AK167857 mRNA. Translation: BAE39875.1 .
    AK168239 mRNA. Translation: BAE40189.1 .
    AK169043 mRNA. Translation: BAE40832.1 .
    AK169701 mRNA. Translation: BAE41314.1 .
    BC080685 mRNA. Translation: AAH80685.1 .
    CCDSi CCDS17383.1.
    RefSeqi NP_001028472.2. NM_001033300.2.
    UniGenei Mm.331051.
    Mm.394565.
    Mm.490620.

    3D structure databases

    ProteinModelPortali Q3THK7.
    SMRi Q3THK7. Positions 23-693.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 230837. 2 interactions.
    STRINGi 10090.ENSMUSP00000029405.

    Chemistry

    BindingDBi Q3THK7.
    ChEMBLi CHEMBL2765.

    Protein family/group databases

    MEROPSi C26.950.

    PTM databases

    PhosphoSitei Q3THK7.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00351252.

    Proteomic databases

    MaxQBi Q3THK7.
    PaxDbi Q3THK7.
    PRIDEi Q3THK7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029405 ; ENSMUSP00000029405 ; ENSMUSG00000027823 .
    GeneIDi 229363.
    KEGGi mmu:229363.
    UCSCi uc008pke.1. mouse.

    Organism-specific databases

    CTDi 8833.
    MGIi MGI:2448526. Gmps.

    Phylogenomic databases

    eggNOGi COG0519.
    GeneTreei ENSGT00390000006591.
    HOGENOMi HOG000223965.
    HOVERGENi HBG005929.
    InParanoidi Q3THK7.
    KOi K01951.
    OMAi GTVHKKN.
    OrthoDBi EOG7J17Z9.
    PhylomeDBi Q3THK7.
    TreeFami TF106132.

    Enzyme and pathway databases

    UniPathwayi UPA00189 ; UER00296 .

    Miscellaneous databases

    NextBioi 379420.
    PROi Q3THK7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q3THK7.
    Bgeei Q3THK7.
    CleanExi MM_GMPS.
    Genevestigatori Q3THK7.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    3.40.50.880. 1 hit.
    InterProi IPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR001674. GMP_synth_C.
    IPR004739. GMP_synth_N.
    IPR025777. GMPS_ATP_PPase_dom.
    IPR022310. NAD/GMP_synthase.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    Pfami PF00117. GATase. 1 hit.
    PF00958. GMP_synt_C. 1 hit.
    PF02540. NAD_synthase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52317. SSF52317. 1 hit.
    TIGRFAMsi TIGR00888. guaA_Nterm. 1 hit.
    PROSITEi PS51273. GATASE_TYPE_1. 1 hit.
    PS51553. GMPS_ATP_PPASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: BALB/c, C57BL/6J, DBA/2 and NOD.
      Tissue: Eye, Heart, Kidney, Spinal cord and Thymus.
    2. "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] OF 217-693.
      Tissue: Limb.
    3. Lubec G., Klug S., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 536-548 AND 570-589, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Hippocampus.

    Entry informationi

    Entry nameiGUAA_MOUSE
    AccessioniPrimary (citable) accession number: Q3THK7
    Secondary accession number(s): Q3TFR6
    , Q3TIH1, Q3UJ21, Q3V343, Q66JZ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 17, 2007
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 93 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, Direct protein sequencing, 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