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Reviewed, UniProtKB/Swiss-Prot O05269 (GUAC_BACSU)

Last modified February 9, 2010. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Synonyms: yumD
Ordered Locus Names: BSU32130
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 Probable. Ref.4

Catalytic activity

Inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH. HAMAP MF_01511

Induction

Expression is regulated by purR. Ref.4

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: UniProtKB-KW

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 HAMAP MF_01511
PRO_0000093752

Regions

Nucleotide binding204 – 22724NADP By similarity

Sites

Active site1751Thioimidate intermediate By similarity

Experimental info

Sequence conflict2621Q → P in CAB07955. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O05269-1 [UniParc].

Last modified July 28, 2009. Version 2.
Checksum: 4CEF76F398E1D353

FASTA32635,850
        10         20         30         40         50         60 
MENVFDYEDI QLIPAKCIVN SRSECDTSVR LGGHTFKLPV VPANMQTIID EKLAISLAEN 

        70         80         90        100        110        120 
GYFYVMHRFE PETRIDFIKD MNARGLFSSI SVGVKDEEYE FVRQLAEENL TPEYVTIDIA 

       130        140        150        160        170        180 
HGHSNAVIEM IQHLKKHLPD SFVIAGNVGT PEAVRELENA GADATKVGIG PGKVCITKIK 

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

       250        260        270        280        290        300 
GQTIEKDGKL YKEYFGSASE FQKGEKKNVE GKKMHVAHKG SIKDTLIEME QDLQSSISYA 

       310        320 
GGTKLNAIRN VDYVIVKNSI FNGDKY 

« Hide

References

« Hide 'large scale' references
[1]Oudega B., Koningstein G., de Sales Ramon M., Rodrigues L.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract]
Cited for: SEQUENCE REVISION TO 262.
[4]"Definition of the Bacillus subtilis PurR operator using genetic and bioinformatic tools and expansion of the PurR regulon with glyA, guaC, pbuG, xpt-pbuX, yqhZ-folD, and pbuO."
Saxild H.H., Brunstedt K., Nielsen K.I., Jarmer H., Nygaard P.
J. Bacteriol. 183:6175-6183(2001) [PubMed: 11591660] [Abstract]
Cited for: PROBABLE FUNCTION, REGULATION OF EXPRESSION.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z93939 Genomic DNA. Translation: CAB07955.1.
AL009126 Genomic DNA. Translation: CAB15203.2.
PIRC70015.
RefSeqNP_391093.2.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID937189.
GenomeReviewsGene locus BSU32130 in contig AL009126_GR.
KEGGbsu:BSU32130.
NMPDRfig|224308.1.peg.3219.

Organism-specific databases

SubtiListBG12392. guaC. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMHBG298985.
PhylomeDBO05269.

Enzyme and pathway databases

BioCycSUBTI:BSU32130-MONOMER.
BRENDA1.7.1.7. 150.

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.
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_BACSU
AccessionPrimary (citable) accession number: O05269
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: July 28, 2009
Last modified: February 9, 2010
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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