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Reviewed, UniProtKB/Swiss-Prot Q65LF6 (GUAC_BACLD)

Last modified November 25, 2008. Version 27. 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: BLi01200, BL05105
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length326 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 – 326326GMP reductase
PRO_0000093751

Regions

Nucleotide binding204 – 22724NADP Potential

Sites

Active site1751Thioimidate intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65LF6-1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 9767F95E143A670E

FASTA32635,893
        10         20         30         40         50         60 
MENVFDYEDI QLIPAKCIVK SRSECDTSVQ FGGRTFKLPV VPANMQTIID EKLAVSLAEN 

        70         80         90        100        110        120 
GYFYVMHRFE PETRIDFIKD MKARGLFSSI SVGVKDEEYA FIEELTRENL TPEYITIDIA 

       130        140        150        160        170        180 
HGHSNAVINM IQHIKKHLPD SFVIAGNVGT PEAVRELENA GADATKVGIG PGKVCITKIK 

       190        200        210        220        230        240 
TGFGTGGWQL AALRWCAKAA SKPIIADGGI RTHGDIAKSV RFGATMVMIG SLFAGHEESP 

       250        260        270        280        290        300 
GATIEKDGKL YKEYFGSASE YQKGEKKNVE GKKMYVEHKG AIMDTLTEME QDLQSSISYA 

       310        320 
GGNKLDAIRN VDYVIVKNSI FNGDQY 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE017333 Genomic DNA. Translation: AAU40108.1.
CP000002 Genomic DNA. Translation: AAU22762.1.
RefSeqYP_078400.1.
YP_090801.1.

3D structure databases

SMRQ65LF6. Positions 1-321.
ModBaseSearch...

Genome annotation databases

GeneID3030188.
3099019.
GenomeReviewsGene locus BL05105 in contig CP000002_GR.
Gene locus BLi01200 in contig AE017333_GR.
KEGGbld:BLi01200.
bli:BL05105.
NMPDRfig|279010.5.peg.2281.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ65LF6.

Enzyme and pathway databases

BioCycBLIC279010:BL05105-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_BACLD
AccessionPrimary (citable) accession number: Q65LF6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: October 25, 2004
Last modified: November 25, 2008
This is version 27 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