Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C0MF02 (GUAC_STRS7) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 35. 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:SZO_09290
OrganismStreptococcus equi subsp. zooepidemicus (strain H70) [Complete proteome] [HAMAP]
Taxonomic identifier553483 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length327 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_01511

Catalytic activity

Inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH. HAMAP-Rule MF_01511

Sequence similarities

Belongs to the IMPDH/GMPR family. GuaC type 2 subfamily.

Ontologies

Keywords
   LigandNADP
   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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327GMP reductase HAMAP-Rule MF_01511
PRO_1000215346

Regions

Nucleotide binding205 – 22824NADP Potential

Sites

Active site1761Thioimidate intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
C0MF02 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: 80272EDE371C05A6

FASTA32736,190
        10         20         30         40         50         60 
MFNDMPVFDY EDIQLIPNKC IINSRSEADT SVRLGNYTFK LPVIPANMQT IIDETIAEQL 

        70         80         90        100        110        120 
ARDGYFYIMH RFDEQGRKPF IQRMHEQQLI ASISVGVKDY EYDFVSSLKE DAPEFITIDI 

       130        140        150        160        170        180 
AHGHADSVIK MIKHIKAELP ETFVIAGNVG TPEAVRELEN AGADATKVGI GPGKVCITKV 

       190        200        210        220        230        240 
KTGFGTGGWQ LAAVRWCAKA ARKPIIADGG IRTHGDIAKS IRFGATMVMI GSLFAGHIES 

       250        260        270        280        290        300 
PGKMVEIDGQ SFKEYYGSAS EYQKGEHKNV EGKKILLPTK GHLADTLTEM KQDLQSSISY 

       310        320 
AGGRELESLR RVNYVIVKNS IWNGDSI 

« Hide

References

[1]"Genomic evidence for the evolution of Streptococcus equi: host restriction, increased virulence, and genetic exchange with human pathogens."
Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F., Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M., Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A. expand/collapse author list , Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C., Maskell D.J., Parkhill J., Waller A.S.
PLoS Pathog. 5:E1000346-E1000346(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: H70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM204884 Genomic DNA. Translation: CAW99190.1.
RefSeqYP_002744456.1. NC_012470.1.

3D structure databases

ProteinModelPortalC0MF02.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING553483.SZO_09290.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAW99190; CAW99190; SZO_09290.
GeneID7695264.
KEGGseq:SZO_09290.
PATRIC19651578. VBIStrEqu35012_0986.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0516.
HOGENOMHOG000165753.
KOK00364.
OMAPDYITID.
OrthoDBEOG6GTZPV.
ProtClustDBPRK05458.

Enzyme and pathway databases

BioCycSEQU40041:GC8B-1009-MONOMER.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01511. GMP_reduct_type2.
InterProIPR013785. Aldolase_TIM.
IPR005994. GMP_reduct2.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PfamPF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFPIRSF036500. GMP_red_Firmic. 1 hit.
TIGRFAMsTIGR01306. GMP_reduct_2. 1 hit.
PROSITEPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUAC_STRS7
AccessionPrimary (citable) accession number: C0MF02
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 5, 2009
Last modified: February 19, 2014
This is version 35 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