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Q3THK7

- GUAA_MOUSE

UniProt

Q3THK7 - GUAA_MOUSE

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Protein

GMP synthase [glutamine-hydrolyzing]

Gene

Gmps

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00189; UER00296.

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-KW
Complete GO annotation...

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

BgeeiQ3THK7.
CleanExiMM_GMPS.
ExpressionAtlasiQ3THK7. baseline and differential.
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

« Hide

        10         20         30         40         50
MALCNGDSKP ENAGGDLKDG SHHYEGAVVI LDAGAQYGKV IDRRVRELFV
60 70 80 90 100
QSEIFPLETP AFAIKEQGFR AIIISGGPNS VYAEDAPWFD PAIFTIGKPI
110 120 130 140 150
LGICYGMQMM NKVFGGTVHK KSVREDGVFN ISMDNTCSLF RGLQKEEIVL
160 170 180 190 200
LTHGDSVDKV ADGFKVVARS GNIVAGIANE SKKLYGVQFH PEVGLTENGK
210 220 230 240 250
VILKNFLYDI AGCSGNFTVQ NRELECIREI KEKVGTSKVL VLLSGGVDST
260 270 280 290 300
VCTALLNRAL NQDQVIAVHI DNGFMRKRES QSVEEALKKL GIQVKVINAA
310 320 330 340 350
HSFYNGTTTL PISDEDRTPR KRISKTLNMT TSPEEKRKII GDTFVKIANE
360 370 380 390 400
VIGEMSLKPE EVFLAQGTLR PDLIESASLV ASGKAELIKT HHNDTELIRK
410 420 430 440 450
LREEGKVIEP LKDFHKDEVR ILGRELDLPE ELVSRHPFPG PGLAIRVICA
460 470 480 490 500
EEPYICKDFP ETNNILKIVA DFSASVKKPH TLLQRVKACT TEEDQEKLMQ
510 520 530 540 550
ITSLHSLNAF LLPIKTVGVQ GDCRSYSYVC GISSKDEPDW ESLIFLARLI
560 570 580 590 600
PRMCHNINRV VYIFGPPVKE PPTDVTPTFL TTGVLSTLRQ ADFEAHNILR
610 620 630 640 650
ESGFAGKISQ MPVILTPLHF DRDPLQKQPS CQRSVVIRTF ITSDFMTGVP
660 670 680 690
ATPGNEIPVE VVLKMVTEIK KIPGISRIMY DLTSKPPGTT EWE
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.

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

Bgeei Q3THK7.
CleanExi MM_GMPS.
ExpressionAtlasi Q3THK7. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 94 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