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Reviewed, UniProtKB/Swiss-Prot Q814I1 (GUAC_BACCR)

Last modified November 25, 2008. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: BC_5452
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Complete proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

Inosine 5'-phosphate + NH(3) + NADP(+) = guanosine 5'-phosphate + NADPH.

Sequence similarities

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

Ontologies

Keywords

   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: InterPro

purine nucleotide metabolic process

Inferred from electronic annotation. Source: HAMAP

   Molecular functionGMP reductase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 328328GMP reductase
PRO_0000093748

Regions

Nucleotide binding205 – 22824NADP By similarity

Sites

Active site1761Thioimidate intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q814I1-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 10CD18A4A129E81D

FASTA32836,306
        10         20         30         40         50         60 
MMENVFDYED IQLIPAKCIV NSRSECDTTV TLGKHKFKLP VVPANMQTII DERIATYLAE 

        70         80         90        100        110        120 
NNYFYIMHRF QPEKRISFIR DMQSRGLIAS ISVGVKEDEY EFVQQLAAEQ LTPEYITIDI 

       130        140        150        160        170        180 
AHGHSNAVIN MIQHIKKHLP ESFVIAGNVG TPEAVRELEN AGADATKVGI GPGKVCITKI 

       190        200        210        220        230        240 
KTGFGTGGWQ LAALRWCAKA ASKPIIADGG IRTHGDVAKS IRFGATMVMI GSLFAGHEES 

       250        260        270        280        290        300 
PGETIERDGK LYKEYFGSAS EFQKGEKKNV EGKKMFVEHK GSLEDTLIEM EQDLQSSISY 

       310        320 
AGGTKLDAIR TVDYVVVKNS IFNGDKVY 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed: 12721630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE016877 Genomic DNA. Translation: AAP12313.1.
RefSeqNP_835112.1.

3D structure databases

HSSPHSSP built from PDB template 1EEP based on UniProtKB P49058.
SMRQ814I1. Positions 2-322.
ModBaseSearch...

Genome annotation databases

GeneID1207792.
GenomeReviewsGene locus BC_5452 in contig AE016877_GR.
KEGGbce:BC5452.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ814I1.

Enzyme and pathway databases

BioCycBCER226900:BC_5452-MON.

Family and domain databases

HAMAPMF_01511.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR005994. GMP_reduct2.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DHase_GMPRtase.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
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_BACCR
AccessionPrimary (citable) accession number: Q814I1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: June 1, 2003
Last modified: November 25, 2008
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents