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B9DS39 (GUAC_STRU0) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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:SUB0865
OrganismStreptococcus uberis (strain ATCC BAA-854 / 0140J) [Complete proteome] [HAMAP]
Taxonomic identifier218495 [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_1000185058

Regions

Nucleotide binding205 – 22824NADP Potential

Sites

Active site1761Thioimidate intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
B9DS39 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 478D2C47193A9BFA

FASTA32736,119
        10         20         30         40         50         60 
MFNDMPVFDY EDIQLIPNKC IINSRSEADT SVQLGKYSFK LPVIPANMQT IIDETIAEQL 

        70         80         90        100        110        120 
AKDGYFYIMH RFDEESRKPF IKRMHEQNLI ASISVGVKEY EYDFVTSLKE DAPEFVTIDI 

       130        140        150        160        170        180 
AHGHANSVIK MIQHIKKELP ETFVIAGNVG TPEAVRELEN AGADATKVGI GPGKVCITKV 

       190        200        210        220        230        240 
KTGFGTGGWQ LAALRWCAKA ARKPIIADGG IRTHGDIAKS IRFGATMVMI GSLFAGHLES 

       250        260        270        280        290        300 
PGKLVEIDGE TFKEYYGSAS EYQKGEHKNV EGKKILLPTK GHLSDTLTEM KQDLQSSISY 

       310        320 
AGGNDLAALR RVDYVIVKNS IWNGDSI 

« Hide

References

[1]"Evidence for niche adaptation in the genome of the bovine pathogen Streptococcus uberis."
Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A., Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R., Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D., Parkhill J.
BMC Genomics 10:54-54(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-854 / 0140J.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM946015 Genomic DNA. Translation: CAR41922.1.
RefSeqYP_002562194.1. NC_012004.1.

3D structure databases

ProteinModelPortalB9DS39.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218495.SUB0865.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR41922; CAR41922; SUB0865.
GeneID7391352.
KEGGsub:SUB0865.
PATRIC19807426. VBIStrUbe20775_0833.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSUBE218495:GJ7D-904-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_STRU0
AccessionPrimary (citable) accession number: B9DS39
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: February 19, 2014
This is version 36 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