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Q3THK7 (GUAA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GMP synthase [glutamine-hydrolyzing]
EC=6.3.5.2
Alternative name(s):
GMP synthetase
Glutamine amidotransferase
Gene names
Name:Gmps
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length693 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate.

Pathway

Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Contains 1 glutamine amidotransferase type-1 domain.

Contains 1 GMPS ATP-PPase (ATP pyrophosphatase) domain.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 693692GMP synthase [glutamine-hydrolyzing]
PRO_0000284365

Regions

Domain27 – 216190Glutamine amidotransferase type-1
Domain217 – 435219GMPS ATP-PPase
Nucleotide binding244 – 2507ATP By similarity

Sites

Active site1041For GATase activity By similarity
Active site1901For GATase activity By similarity
Active site1921For GATase activity By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue91N6-acetyllysine By similarity
Modified residue3181Phosphothreonine By similarity
Modified residue3321Phosphoserine Ref.4

Experimental info

Sequence conflict2011V → I in BAE39875. Ref.1
Sequence conflict2051N → Y in BAE39875. Ref.1
Sequence conflict2651V → D in BAE39875. Ref.1
Sequence conflict3561S → G in BAE40189. Ref.1
Sequence conflict3591P → H in BAE40189. Ref.1
Sequence conflict3591P → R in BAE39875. Ref.1
Sequence conflict3631Missing in BAE39875. Ref.1
Sequence conflict511 – 5122LL → CC in BAE27334. Ref.1
Sequence conflict5861S → G in BAE39875. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3THK7 [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: 854DBAD6A9C75A12

FASTA69376,723
        10         20         30         40         50         60 
MALCNGDSKP ENAGGDLKDG SHHYEGAVVI LDAGAQYGKV IDRRVRELFV QSEIFPLETP 

        70         80         90        100        110        120 
AFAIKEQGFR AIIISGGPNS VYAEDAPWFD PAIFTIGKPI LGICYGMQMM NKVFGGTVHK 

       130        140        150        160        170        180 
KSVREDGVFN ISMDNTCSLF RGLQKEEIVL LTHGDSVDKV ADGFKVVARS GNIVAGIANE 

       190        200        210        220        230        240 
SKKLYGVQFH PEVGLTENGK VILKNFLYDI AGCSGNFTVQ NRELECIREI KEKVGTSKVL 

       250        260        270        280        290        300 
VLLSGGVDST VCTALLNRAL NQDQVIAVHI DNGFMRKRES QSVEEALKKL GIQVKVINAA 

       310        320        330        340        350        360 
HSFYNGTTTL PISDEDRTPR KRISKTLNMT TSPEEKRKII GDTFVKIANE VIGEMSLKPE 

       370        380        390        400        410        420 
EVFLAQGTLR PDLIESASLV ASGKAELIKT HHNDTELIRK LREEGKVIEP LKDFHKDEVR 

       430        440        450        460        470        480 
ILGRELDLPE ELVSRHPFPG PGLAIRVICA EEPYICKDFP ETNNILKIVA DFSASVKKPH 

       490        500        510        520        530        540 
TLLQRVKACT TEEDQEKLMQ ITSLHSLNAF LLPIKTVGVQ GDCRSYSYVC GISSKDEPDW 

       550        560        570        580        590        600 
ESLIFLARLI PRMCHNINRV VYIFGPPVKE PPTDVTPTFL TTGVLSTLRQ ADFEAHNILR 

       610        620        630        640        650        660 
ESGFAGKISQ MPVILTPLHF DRDPLQKQPS CQRSVVIRTF ITSDFMTGVP ATPGNEIPVE 

       670        680        690 
VVLKMVTEIK KIPGISRIMY DLTSKPPGTT EWE

« Hide

References

« Hide 'large scale' references
[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. 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: 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, MASS SPECTROMETRY.
Tissue: Brain and Hippocampus.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00351252.
RefSeqNP_001028472.2. NM_001033300.2.
UniGeneMm.331051.
Mm.394565.
Mm.490620.

3D structure databases

ProteinModelPortalQ3THK7.
SMRQ3THK7. Positions 23-693.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000029405.

Protein family/group databases

MEROPSC26.950.

PTM databases

PhosphoSiteQ3THK7.

2D gel databases

REPRODUCTION-2DPAGEIPI00351252.

Proteomic databases

PaxDbQ3THK7.
PRIDEQ3THK7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029405; ENSMUSP00000029405; ENSMUSG00000027823.
GeneID229363.
KEGGmmu:229363.
UCSCuc008pke.1. mouse.

Organism-specific databases

CTD8833.
MGIMGI:2448526. Gmps.

Phylogenomic databases

eggNOGCOG0519.
GeneTreeENSGT00390000006591.
HOGENOMHOG000223965.
HOVERGENHBG005929.
InParanoidQ3THK7.
KOK01951.
OMANMTTNPE.
OrthoDBEOG4J6RQ9.

Enzyme and pathway databases

UniPathwayUPA00189; UER00296.

Gene expression databases

ArrayExpressQ3THK7.
BgeeQ3THK7.
CleanExMM_GMPS.
GenevestigatorQ3THK7.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
InterProIPR017926. 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]
PfamPF00117. GATase. 1 hit.
PF00958. GMP_synt_C. 1 hit.
PF02540. NAD_synthase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00888. guaA_Nterm. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
PS51553. GMPS_ATP_PPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ3THK7.
ChEMBLCHEMBL2765.
NextBio379420.
SOURCESearch...

Entry information

Entry nameGUAA_MOUSE
AccessionPrimary (citable) accession number: Q3THK7
Secondary accession number(s): Q3TFR6 expand/collapse secondary AC list , Q3TIH1, Q3UJ21, Q3V343, Q66JZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: May 29, 2013
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents