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Reviewed, UniProtKB/Swiss-Prot Q81JJ9 (GUAC_BACAN)

Last modified November 25, 2008. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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: BA_5705, GBAA5705, BAS5309
OrganismBacillus anthracis [Complete proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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 term3D-structure
Complete 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 – 327327GMP reductase
PRO_0000093746

Regions

Nucleotide binding204 – 22724NADP By similarity

Sites

Active site1751Thioimidate intermediate By similarity

Secondary structure

...................................................... 327
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q81JJ9-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 8006FDFA6A5F2E78

FASTA32736,076
        10         20         30         40         50         60 
MGNVFDYEDI QLIPAKCIVN SRSECDTTVT LGKHKFKLPV VPANMQTIID ERIATYLAEN 

        70         80         90        100        110        120 
NYFYIMHRFQ PEKRISFIRD MQSRGLIASI SVGVKEDEYE FVQQLAAEHL TPEYITIDIA 

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

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

       250        260        270        280        290        300 
GETIEKDGKL YKEYFGSASE FQKGEKKNVE GKKMFVEHKG SLEDTLIEME QDLQSSISYA 

       310        320 
GGTKLDSIRT VDYVVVKNSI FNGDKVY 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.

Cross-references

Sequence databases

AE016879 Genomic DNA. Translation: AAP29337.1.
AE017334 Genomic DNA. Translation: AAT34865.1.
AE017225 Genomic DNA. Translation: AAT57596.1.
RefSeqNP_847851.1.
YP_022390.1.
YP_031546.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1YPFX-ray1.80A/B1-327[»]
2A1YX-ray2.27A1-327[»]
ModBaseSearch...

Genome annotation databases

GeneID1085456.
2816139.
2852911.
GenomeReviewsGene locus BA_5705 in contig AE016879_GR.
Gene locus BAS5309 in contig AE017225_GR.
Gene locus GBAA5705 in contig AE017334_GR.
KEGGban:BA5705.
bar:GBAA5705.
bat:BAS5309.
TIGRBA_5705.
GBAA5705.

Phylogenomic databases

HOGENOMQ81JJ9.

Enzyme and pathway databases

BioCycBANT260799:BAS5309-MON.
BANT261594:GBAA5705-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_BACAN
AccessionPrimary (citable) accession number: Q81JJ9
Secondary accession number(s): Q6HQ42, Q6KJI6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: June 1, 2003
Last modified: November 25, 2008
This is version 45 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

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