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Q65LF6 (GUAC_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. 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:BLi01200, BL05105
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length326 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_01511

Catalytic activity

Inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH. HAMAP 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: InterPro

   Molecular functionGMP reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 326326GMP reductase HAMAP MF_01511
PRO_0000093751

Regions

Nucleotide binding204 – 22724NADP Potential

Sites

Active site1751Thioimidate intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65LF6 [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].
Strain: DSM 13 / ATCC 14580.
[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:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017333 Genomic DNA. Translation: AAU40108.1.
CP000002 Genomic DNA. Translation: AAU22762.1.
RefSeqYP_078400.1. NC_006270.3.
YP_090801.1. NC_006322.1.

3D structure databases

ProteinModelPortalQ65LF6.
SMRQ65LF6. Positions 1-321.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ65LF6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000054478; EBBACP00000053009; EBBACG00000054469.
EBBACT00000060372; EBBACP00000058805; EBBACG00000060363.
GeneID3030188.
3099019.
GenomeReviewsGene locus BLi01200 in contig AE017333_GR.
Gene locus BL05105 in contig CP000002_GR.
KEGGbld:BLi01200.
bli:BL05105.
NMPDRfig|279010.5.peg.2281.
PATRIC18947967. VBIBacLic203714_1188.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0516.
GeneTreeEBGT00050000000995.
HOGENOMHBG298985.
OMAPDYITID.
ProtClustDBPRK05458.

Enzyme and pathway databases

BioCycBLIC279010-1:BLI01200-MONOMER.
BLIC279010:BL05105-MONOMER.

Family and domain databases

HAMAPMF_01511. GMP_reduct_type2.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR005994. GMP_reduct2.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK00364.
PANTHERPTHR11911:SF30. PTHR11911:SF30. 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: January 25, 2012
This is version 48 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