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C4LAB3 (GUAC_TOLAT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 31. 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:Tola_2494
OrganismTolumonas auensis (strain DSM 9187 / TA4) [Complete proteome] [HAMAP]
Taxonomic identifier595494 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeTolumonas

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_1000212182

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
C4LAB3 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: D6640907D10ADBE0

FASTA34737,709
        10         20         30         40         50         60 
MRIEEDLKLG FKDVLFRPKR STLSSRSQVE LHREFRFRHT QTSWRGVPII AANMDTVGTF 

        70         80         90        100        110        120 
AMAKALASFD VMTAIHKHYT EQEWQTFVQN SSDPLLQYCM VSTGTSNNDF LKLQRILALS 

       130        140        150        160        170        180 
PALRFICVDV ANGYSEHFAD FVKIVRETFP QHVICAGNVV TGEMVEELIL SGADIVKVGI 

       190        200        210        220        230        240 
GPGSVCTTRV KTGVGYPQLS AIIECADAAH GLGGQIVGDG GCTCPGDVAK AFGGGADFVM 

       250        260        270        280        290        300 
LGGMLAAHEE SGGNKFERDG KTFMRFYGMS SSTAMEQHAG GIAHYRASEG KTVELPFRGP 

       310        320        330        340 
VSATIQDILG GVRSTCTYVG AAKLKELTKR TTFIRVSEQE NPVYGQE 

« Hide

References

[1]"Complete sequence of Tolumonas auensis DSM 9187."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S., Beller H.
Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 9187 / TA4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001616 Genomic DNA. Translation: ACQ94088.1.
RefSeqYP_002893674.1. NC_012691.1.

3D structure databases

ProteinModelPortalC4LAB3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING595494.Tola_2494.

Proteomic databases

PRIDEC4LAB3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ94088; ACQ94088; Tola_2494.
GeneID7885219.
KEGGtau:Tola_2494.
PATRIC23981659. VBITolAue42623_2478.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycTAUE595494:GHEF-2575-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_TOLAT
AccessionPrimary (citable) accession number: C4LAB3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 7, 2009
Last modified: February 19, 2014
This is version 31 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