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Q2FL30 (GUAAA_METHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
GMP synthase [glutamine-hydrolyzing] subunit A

EC=6.3.5.2
Alternative name(s):
Glutamine amidotransferase
Gene names
Name:guaAA
Ordered Locus Names:Mhun_1588
OrganismMethanospirillum hungatei (strain JF-1 / DSM 864)
Taxonomic identifier323259 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanospirillaceaeMethanospirillum

Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the synthesis of GMP from XMP By similarity. HAMAP MF_01510

Catalytic activity

ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate. HAMAP MF_01510

Pathway

Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. HAMAP MF_01510

Subunit structure

Heterodimer composed of a glutamine amidotransferase subunit (A) and a GMP-binding subunit (B) Potential.

Sequence similarities

Contains 1 glutamine amidotransferase type-1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 188188GMP synthase [glutamine-hydrolyzing] subunit A HAMAP MF_01510
PRO_0000294268

Regions

Domain3 – 188186Glutamine amidotransferase type-1

Sites

Active site751Nucleophile By similarity
Active site1621 By similarity
Active site1641 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2FL30 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: EDA84824871ADEF0

FASTA18820,428
        10         20         30         40         50         60 
MLPLYVVNNY GQFNHLILRA LRDLDIDAKL IPNTTPVSEV REGCQGIILG GGPDISRAGL 

        70         80         90        100        110        120 
SHEYVRLGKP VLGICLGLHV IAQEFGGTVQ SGQKGGYGAV EVTITDHDGI LQGYPQTMQV 

       130        140        150        160        170        180 
WASHADEVVT LPGDFDRLAT SSICGNEAIA HKHLPIFGIQ WHPEVSHTFE GHRVFENFFS 


ICTGQNKG 

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References

[1]"Complete sequence of Methanospirillum hungatei JF-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Ivanova N., McInerney M.J., Brockman F., Culley D., Ferry J.G., Gunsalus R.P., Morrison M., Plugge C., Scholten J., Stams A.J.M., Boone D.R., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JF-1 / DSM 864.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000254 Genomic DNA. Translation: ABD41319.1.
RefSeqYP_503038.1. NC_007796.1.

3D structure databases

ProteinModelPortalQ2FL30.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2FL30.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3923844.
GenomeReviewsGene locus Mhun_1588 in contig CP000254_GR.
KEGGmhu:Mhun_1588.
NMPDRfig|323259.5.peg.1684.

Phylogenomic databases

eggNOGarNOG05587.
HOGENOMHBG292341.
OMAGQYVHRI.
ProtClustDBPRK00758.

Enzyme and pathway databases

BioCycMHUN323259:MHUN_1588-MONOMER.

Family and domain databases

HAMAPMF_01510. GMP_synthase_A.
[Tree]
InterProIPR017926. GATASE_1.
IPR004739. GMP_synth_N.
IPR023686. GMP_synthase_A.
[Graphical view]
KOK01951.
PfamPF00117. GATase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00888. GuaA_Nterm. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUAAA_METHJ
AccessionPrimary (citable) accession number: Q2FL30
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: March 21, 2006
Last modified: January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families