ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry O16294

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name GMPR_CAEEL
Primary accession number O16294
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 55)
Name and origin of the protein
Protein name Probable GMP reductase
Synonyms EC 1.7.1.7
Guanosine 5'-monophosphate oxidoreductase
Guanosine monophosphate reductase
Gene name
ORFNames: F32D1.5
From
Caenorhabditis elegans [TaxID: 6239] 
Taxonomy Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
DOI=10.1126/science.282.5396.2012; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan]
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for investigating biology.";
Science 282:2012-2018(1998).
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 + NH3 + NADP+ = guanosine 5'-phosphate + NADPH.
  • SIMILARITY: Belongs to the IMPDH/GMPR family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF016427; AAB65350.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T03917; T03917.
RefSeq NP_504202.1; -.
UniGene Cel.6523
3D structure databases
HSSP P49058; 1EEP. [HSSP ENTRY / PDB]
SMR O16294; 2-339.
ModBase O16294.
Organism-specific databases
WormBase WBGene00017984; F32D1.5.
WormPep F32D1.5; CE09869. [WormPep / WorfDB]
Gene expression databases
ArrayExpress O16294; -.
Family and domain databases
InterPro IPR013785; Aldolase_TIM.
IPR005993; GMP_reduct1.
IPR015875; IMP_DH/GMP_Rdtase_CS.
IPR001093; IMP_DHase_GMPRtase.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Pfam PF00478; IMPDH; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000235; GMP_reductase; 1.
TIGRFAMs TIGR01305; GMP_reduct_1; 1.
PROSITE PS00487; IMP_DH_GMP_RED; 1.
BLOCKS O16294.
Genome annotation databases
Ensembl F32D1.5; Caenorhabditis elegans. [Contig view]
GeneID 178834; -.
KEGG cel:F32D1.5; -.
Other
ProtoNet O16294.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Metal-binding; NADP; Oxidoreductase; Potassium.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   358  358     Probable GMP reductase. PRO_0000093729
NP_BIND   109   132  24     NADP (By similarity). 
ACT_SITE   187   187        Thioimidate intermediate (By similarity). 
METAL   182   182        Potassium (via carbonyl oxygen) (By similarity). 
METAL   184   184        Potassium (via carbonyl oxygen) (By similarity). 
BINDING   220   220        NADP (By similarity). 
Sequence information
Length: 358 AA [This is the length of the unprocessed precursor] Molecular weight: 38806 Da [This is the MW of the unprocessed precursor] CRC64: A4AEE84F2CB72360 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MPRIENEPKL DFKDVLLRPK RSTLKSRADV ELDREYVFRN SKATYTGVPV VASNMDTVGT 

        70         80         90        100        110        120 
FEMAAALNNH KIFTTIHKHY SVDEWKAFAA SASPDTFNNL AISSGISDND WTKLNTVITE 

       130        140        150        160        170        180 
LPQLKYICLD VANGYSESFV EFIRRVREAY PKHTIMAGNV VTGEMVEELI LSGADIVKVG 

       190        200        210        220        230        240 
IGPGSVCTTR KKAGVGYPQL SAVLECADAA HGLNGHVMSD GGCSNPGDVA KAFGAGADFV 

       250        260        270        280        290        300 
MIGGLFAGHD QSGGDLIEHN GKKFKLFYGM SSDTAMKKHH GSVAEYRASE GKTVTIPYRG 

       310        320        330        340        350 
DVNGTVQDIL GGIRSACTYT GAKHLKELAK RATFIRVTQQ TNDMYVPFEV PTVPAPSK
O16294 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!