GMP synthase [glutamine-hydrolyzing]

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Reviewed, UniProtKB/Swiss-Prot P49915 (GUAA_HUMAN)

Last modified June 16, 2009. Version 98. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    GMP synthase [glutamine-hydrolyzing]
    EC=6.3.5.2
Alternative name(s):
    Glutamine amidotransferase
    GMP synthetase

Gene names

Name:

GMPS

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	693 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.
Catalytic activity	ATP + xanthosine 5'-phosphate + L-glutamine + H₂O = AMP + diphosphate + GMP + L-glutamate.
Pathway	Purine metabolism; GMP biosynthesis; GMP from XMP (glutamine route): step 1/1.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm.
Involvement in disease	A chromosomal aberration involving GMPS is found in acute myeloid leukemias. Translocation t(3,11)(q25,q23) with MLL.
Sequence similarities	Contains 1 glutamine amidotransferase type-1 domain. Contains 1 GMP-binding domain.

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Ontologies

Keywords
Biological process	GMP biosynthesis Purine biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Chromosomal rearrangement
Disease	Proto-oncogene
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	GMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW purine base biosynthetic process Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GMP synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: EC GMP synthase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 693

693

GMP synthase [glutamine-hydrolyzing]

PRO_0000140257

Regions

Domain

27 – 216

190

Glutamine amidotransferase type-1

Nucleotide binding

244 – 250

ATP By similarity

Sites

Active site

104

For GATase activity By similarity

Active site

190

For GATase activity By similarity

Active site

192

For GATase activity By similarity

Amino acid modifications

Modified residue

318

Phosphothreonine Ref.4

Modified residue

332

Phosphoserine Ref.5

Experimental info

Sequence conflict

415

H → I AA sequence Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P49915-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 1CDA0DD3B244728D
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FASTA

693

76,715

        10         20         30         40         50         60 
MALCNGDSKL ENAGGDLKDG HHHYEGAVVI LDAGAQYGKV IDRRVRELFV QSEIFPLETP 

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

       130        140        150        160        170        180 
KSVREDGVFN ISVDNTCSLF RGLQKEEVVL LTHGDSVDKV ADGFKVVARS GNIVAGIANE 

       190        200        210        220        230        240 
SKKLYGAQFH PEVGLTENGK VILKNFLYDI AGCSGTFTVQ NRELECIREI KERVGTSKVL 

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

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

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

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

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

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

       610        620        630        640        650        660 
ESGYAGKISQ MPVILTPLHF DRDPLQKQPS CQRSVVIRTF ITSDFMTGIP ATPGNEIPVE 

       670        680        690 
VVLKMVTEIK KIPGISRIMY DLTSKPPGTT EWE

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA." Hirst M., Haliday E., Nakamura J., Lou L. J. Biol. Chem. 269:23830-23837(1994) [PubMed: 8089153] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[3]	"t(3;11) translocation in treatment-related acute myeloid leukemia fuses MLL with the GMPS (guanosine 5-prime monophosphate synthetase) gene." Pegram L.D., Megonigal M.D., Lange B.J., Nowell P.C., Rowley J.D., Rappaport E.F., Felix C.A. Blood 96:4360-4362(2000) [PubMed: 11110714] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH MLL.
[4]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318, MASS SPECTROMETRY. Tissue: Epithelium.
[5]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, MASS SPECTROMETRY.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

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Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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Cross-references

Sequence databases

U10860 mRNA. Translation: AAA60331.1.
BC012178 mRNA. Translation: AAH12178.1.

IPI

IPI00029079.

PIR

A54847.

RefSeq

NP_003866.1.

UniGene

Hs.591314

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VPI	X-ray	2.40	A/B	25-219	[»]
2VXO	X-ray	2.50	A/B	20-693	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P49915. 4 interactions.

Protein family/group databases

MEROPS

C26.950.

PTM databases

PhosphoSite

P49915.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00029079.

Proteomic databases

PeptideAtlas

P49915.

PRIDE

P49915.

Genome annotation databases

Ensembl

ENSG00000163655. Homo sapiens. [Contig view]

GeneID

8833.

KEGG

hsa:8833.

Organism-specific databases

GeneCards

GC03P157071.

H-InvDB

HIX0018176.

HGNC

HGNC:4378. GMPS.

MIM

600358. gene.

PharmGKB

PA28763.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P49915.

HOVERGEN

P49915.

Enzyme and pathway databases

BRENDA

6.3.5.2. 247.

Reactome

REACT_1698. Nucleotide metabolism.

Gene expression databases

ArrayExpress

P49915.

Bgee

P49915.

CleanEx

HS_GMPS.

GermOnline

ENSG00000163655. Homo sapiens.

Family and domain databases

InterPro

IPR006220. Anth_synthII.
IPR011702. GATASE.
IPR017926. GATASE_1.
IPR000991. GATase_class1_C.
IPR001674. GMP_synth_C.
IPR004739. GMP_synth_N.
IPR018317. Queuosine_synth-like.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

Gene3D

G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.

Pfam

PF06508. ExsB. 1 hit.
PF00117. GATase. 1 hit.
PF00958. GMP_synt_C. 1 hit.
[Graphical view]

PRINTS

PR00097. ANTSNTHASEII.
PR00096. GATASE.

TIGRFAMs

TIGR00888. guaA_Nterm. 1 hit.

PROSITE

PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00142. L-Glutamic Acid.
DB00130. L-Glutamine.

NextBio

33152.

SOURCE

Search...

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Entry information

Entry name

GUAA_HUMAN

Accession

Primary (citable) accession number: P49915

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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