Skip Header

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

Q5PDH8 (GUAC_SALPA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. 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:SPA0145
OrganismSalmonella paratyphi A [Complete proteome] [HAMAP]
Taxonomic identifier54388 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

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_1000025617

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
Q5PDH8 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 71223D342F001B45

FASTA34737,139
        10         20         30         40         50         60 
MRIEEDLKLG FKDVLIRPKR STLKSRSDVE LERQFTFKHS GQTWSGVPII AANMDTVGTF 

        70         80         90        100        110        120 
EMAQALAGFD ILTAVHKHYT VEEWAAFINT ASADVLKHVM VSTGTSDADF EKTVQILALN 

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

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

       250        260        270        280        290        300 
LGGMLAGHEE SGGSVVEENG EKFMLFYGMS SESAMNRHVG GVAKYRAAEG KTVKLPLRGP 

       310        320        330        340 
VGNTARDILG GLRSACTYVG ASRLKELTKR TTFIRVQEQE NRIFNSL 

« Hide

References

[1]"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid."
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. expand/collapse author list , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.
Nat. Genet. 36:1268-1274(2004) [PubMed: 15531882] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000026 Genomic DNA. Translation: AAV76178.1.
RefSeqYP_149490.1. NC_006511.1.

3D structure databases

HSSPHSSP built from PDB template 2BZN based on UniProtKB Q9P2T1.
ProteinModelPortalQ5PDH8.
SMRQ5PDH8. Positions 3-338.
ModBaseSearch...

Proteomic databases

PRIDEQ5PDH8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3177417.
GenomeReviewsGene locus SPA0145 in contig CP000026_GR.
KEGGspt:SPA0145.
PATRIC32349385. VBISalEnt134188_0156.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG298985.
OMAFRNSKQM.
ProtClustDBPRK05096.

Enzyme and pathway databases

BioCycSENT295319:SPA0145-MONOMER.

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_SALPA
AccessionPrimary (citable) accession number: Q5PDH8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 4, 2005
Last modified: January 25, 2012
This is version 54 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