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B7UIF3 (GUAC_ECO27) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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 reductase

EC=1.7.1.7
Alternative name(s):
Guanosine 5'-monophosphate oxidoreductase
Short name=Guanosine monophosphate reductase
Gene names
Name:guaC
Ordered Locus Names:E2348C_0108
OrganismEscherichia coli O127:H6 (strain E2348/69 / EPEC) [Complete proteome] [HAMAP]
Taxonomic identifier574521 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides By similarity. HAMAP MF_00596

Catalytic activity

Inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH. HAMAP MF_00596

Subunit structure

Homotetramer By similarity. HAMAP MF_00596

Sequence similarities

Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.

Ontologies

Keywords
   LigandMetal-binding
NADP
Potassium
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processnucleotide metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionGMP reductase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 347347GMP reductase HAMAP MF_00596
PRO_1000146985

Regions

Nucleotide binding108 – 13124NADP By similarity
Nucleotide binding216 – 23924NADP; ribose moiety By similarity

Sites

Active site1861Thioimidate intermediate By similarity
Metal binding1811Potassium; via carbonyl oxygen By similarity
Metal binding1831Potassium; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
B7UIF3 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 898F50DA7FD00441

FASTA34737,384
        10         20         30         40         50         60 
MRIEEDLKLG FKDVLIRPKR STLKSRSDVE LERQFTFKHS GQSWSGVPII AANMDTVGTF 

        70         80         90        100        110        120 
SMASALASFD ILTAVHKHYS VEEWQAFINN SSADVLKHVM VSTGTSDADF EKTKQILDLN 

       130        140        150        160        170        180 
PALNFVCIDV ANGYSEHFVQ FVAKAREAWP TKTICAGNVV TGEMCEELIL SGADIVKVGI 

       190        200        210        220        230        240 
GPGSVCTTRV KTGVGYPQLS AVIECADAAH GLGGMIVSDG GCTTPGDVAK AFGGGADFVM 

       250        260        270        280        290        300 
LGGMLAGHEE SGGRIVEENG EKFMLFYGMS SESAMKRHVG GVAEYRAAEG KTVKLPLRGP 

       310        320        330        340 
VENTARDILG GLRSACTYVG ASRLKELTKR TTFIRVQEQE NRIFNNL 

« Hide

References

[1]"Complete genome sequence and comparative genome analysis of enteropathogenic Escherichia coli O127:H6 strain E2348/69."
Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.
J. Bacteriol. 191:347-354(2009) [PubMed: 18952797] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E2348/69 / EPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM180568 Genomic DNA. Translation: CAS07656.1.
RefSeqYP_002327700.1. NC_011601.1.

3D structure databases

ProteinModelPortalB7UIF3.
SMRB7UIF3. Positions 9-336.
ModBaseSearch...

Protein-protein interaction databases

STRINGB7UIF3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000114493; EBESCP00000106871; EBESCG00000113243.
GeneID7062823.
GenomeReviewsGene locus E2348_C_0108 in contig FM180568_GR.
KEGGecg:E2348C_0108.
PATRIC18339117. VBIEscCol90278_0112.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009443.
HOGENOMHBG298985.
OMAFRNSKQM.
ProtClustDBPRK05096.

Family and domain databases

HAMAPMF_00596. GMP_reduct_type1.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR005993. GMP_reduct1.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK00364.
PANTHERPTHR11911:SF33. PTHR11911:SF33. 1 hit.
PfamPF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFPIRSF000235. GMP_reductase. 1 hit.
TIGRFAMsTIGR01305. GMP_reduct_1. 1 hit.
PROSITEPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUAC_ECO27
AccessionPrimary (citable) accession number: B7UIF3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: January 25, 2012
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families