Skip Header

Contribute Send feedback
Read comments (?) or add your own

B2GJK0 (B2GJK0_KOCRD) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 46. Feed History...

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

Names and origin

Protein namesRecommended name:
GMP synthase [glutamine-hydrolyzing] HAMAP-Rule MF_00344

EC=6.3.5.2 HAMAP-Rule MF_00344
Alternative name(s):
GMP synthetase HAMAP-Rule MF_00344
Glutamine amidotransferase HAMAP-Rule MF_00344
Gene names
Name:guaA HAMAP-Rule MF_00344 EMBL BAG29029.1
Ordered Locus Names:KRH_06820
OrganismKocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201) [Complete proteome] [HAMAP]
Taxonomic identifier378753 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeKocuria

Protein attributes

Sequence length532 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the synthesis of GMP from XMP By similarity. HAMAP-Rule MF_00344 SAAS SAAS022955

Catalytic activity

ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate. HAMAP-Rule MF_00344 SAAS SAAS022955

Pathway

Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. HAMAP-Rule MF_00344 SAAS SAAS022955

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00344 SAAS SAAS022955

Sequence similarities

Contains 1 GMPS ATP-PPase (ATP pyrophosphatase) domain. HAMAP-Rule MF_00344 SAAS SAAS022955

Contains 1 glutamine amidotransferase type-1 domain. HAMAP-Rule MF_00344 SAAS SAAS022955

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain15 – 207193Glutamine amidotransferase type-1 By similarity HAMAP-Rule MF_00344
Domain208 – 406199GMPS ATP-PPase By similarity HAMAP-Rule MF_00344
Nucleotide binding235 – 2417ATP By similarity HAMAP-Rule MF_00344

Sites

Active site921Nucleophile By similarity HAMAP-Rule MF_00344
Active site1811 By similarity HAMAP-Rule MF_00344
Active site1831 By similarity HAMAP-Rule MF_00344

Sequences

Sequence LengthMass (Da)Tools
B2GJK0 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: F2E26EFF27881EFF

FASTA53257,726
        10         20         30         40         50         60 
MTETPDNLSE LEQRPVLVVD YGAQYAQLIA RRVREANVYS EIVPHTWSTE QILQRNPAAL 

        70         80         90        100        110        120 
ILSGGPASVY APGAPQRDAE LFEAGVPVLG ICYGFQVMAA ALGGTVERTG VREYGATTAT 

       130        140        150        160        170        180 
CQDTAVGTLL DGTPDVQTVW MSHGDSVTAA PEGFTTLATT EGAPVAAFEN RERRLYGVQW 

       190        200        210        220        230        240 
HPEVKHSAYG QKILENFLFN GAQLSPTWST GNIIEEQVAA IRAQVGDGKA LCGLSGGVDS 

       250        260        270        280        290        300 
AVAAALVQRA IGDRLTCVLV DHGLMRQDEV EQVEKDYVAA TGVKLHVARE QDRFLEALKG 

       310        320        330        340        350        360 
VTDPETKRKA IGREFIRAFE AAEEKVLRAE AQDGEPVRFL VQGTLYPDVV ESGGGEGAAN 

       370        380        390        400        410        420 
IKSHHNVGGL PEDLQFELVE PLRALFKDEV RAVGRELGLP ENIVGRQPFP GPGLGIRIIG 

       430        440        450        460        470        480 
EVTEHRLDIL RRADAIAREE LTRAGLDDEV WQMPVVLLAD VRSVGVQGDG RTYGHPIVLR 

       490        500        510        520        530 
PVSSEDAMTA DWSRLPSELL ARVSNRITNE VEEINRVVLD VTSKPPGTIE WE 

« Hide

References

[1]"Complete genome sequence of the soil actinomycete Kocuria rhizophila."
Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S., Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
J. Bacteriol. 190:4139-4146(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9341 / DSM 348 / NBRC 103217 / DC2201.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009152 Genomic DNA. Translation: BAG29029.1.
RefSeqYP_001854535.1. NC_010617.1.

3D structure databases

ProteinModelPortalB2GJK0.
ModBaseSearch...

Protein-protein interaction databases

STRING378753.KRH_06820.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG29029; BAG29029; KRH_06820.
GeneID6238045.
KEGGkrh:KRH_06820.
PATRIC22181604. VBIKocRhi5258_0673.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0519.
HOGENOMHOG000223964.
KOK01951.
OMAYDYVVAL.
ProtClustDBPRK00074.

Enzyme and pathway databases

BioCycKRHI378753:GJ8F-696-MONOMER.
UniPathwayUPA00189; UER00296.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00344. GMP_synthase.
InterProIPR017926. GATASE_1.
IPR001674. GMP_synth_C.
IPR004739. GMP_synth_N.
IPR022955. GMP_synthase.
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]
TIGRFAMsTIGR00884. guaA_Cterm. 1 hit.
TIGR00888. guaA_Nterm. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
PS51553. GMPS_ATP_PPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB2GJK0_KOCRD
AccessionPrimary (citable) accession number: B2GJK0
Entry history
Integrated into UniProtKB/TrEMBL: June 10, 2008
Last sequence update: June 10, 2008
Last modified: May 1, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)