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Q1C3T0 (GUAC_YERPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:YPA_2930
OrganismYersinia pestis bv. Antiqua (strain Antiqua) [Complete proteome] [HAMAP]
Taxonomic identifier360102 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

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-Rule MF_00596

Catalytic activity

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

Subunit structure

Homotetramer By similarity. HAMAP-Rule 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_processpurine nucleotide metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentGMP reductase complex

Inferred from electronic annotation. Source: UniProtKB-EC

   Molecular_functionGMP reductase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

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-Rule MF_00596
PRO_1000025625

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
Q1C3T0 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: 4BF8680985AB19DF

FASTA34737,492
        10         20         30         40         50         60 
MRIEEGLKLG FKDVLIRPKR STLKSRSEVA LERQFTFKHS GWNWSGVPII AANMDTVGTF 

        70         80         90        100        110        120 
RMAEVLASFD ILTAVHKHYT LEQWAEFVKR SPESVLRHVM VSTGTSSADF DKMKQILALS 

       130        140        150        160        170        180 
PSLKFICIDV ANGYSEHFVS FLQRAREACP DKVICAGNVV TGEMVEELIL SGADIVKVGI 

       190        200        210        220        230        240 
GPGSVCTTRV KTGVGYPQLS AVIECADAAH GLGGQIVSDG GCSVPGDVAK AFGGGADFVM 

       250        260        270        280        290        300 
LGGMLAGHDE CEGRVVEENG EKFMLFYGMS SESAMKRHVG GVAQYRAAEG KTVKLPLRGS 

       310        320        330        340 
VDNTVRDIMG GLRSACTYVG ASHLKELTKR TTFIRVAEQE NRVFGTD 

« Hide

References

[1]"Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen."
Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M., Worsham P., Chu M.C., Andersen G.L.
J. Bacteriol. 188:4453-4463(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Antiqua.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000308 Genomic DNA. Translation: ABG14892.1.
RefSeqYP_652837.1. NC_008150.1.

3D structure databases

ProteinModelPortalQ1C3T0.
SMRQ1C3T0. Positions 3-338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360102.YPA_2930.

Proteomic databases

PRIDEQ1C3T0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG14892; ABG14892; YPA_2930.
GeneID4122360.
KEGGypa:YPA_2930.
PATRIC18585628. VBIYerPes1796_3612.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0516.
HOGENOMHOG000165756.
KOK00364.
OMACSCAGDV.
OrthoDBEOG6GTZPV.
ProtClustDBPRK05096.

Enzyme and pathway databases

BioCycYPES360102:GHZU-2996-MONOMER.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00596. GMP_reduct_type1.
InterProIPR013785. Aldolase_TIM.
IPR005993. GMP_reduct1.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
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_YERPA
AccessionPrimary (citable) accession number: Q1C3T0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 11, 2006
Last modified: February 19, 2014
This is version 60 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