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]

T03917; T03917.

NP_504202.1; -.

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; -.

Ontologies

GO:0003920;	Molecular function: GMP reductase activity (inferred from electronic annotation from InterPro).
GO:0030955;	Molecular function: potassium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009792;	Biological process: embryonic development ending in birth or egg hatching (inferred from mutant phenotype from WormBase).
GO:0040007;	Biological process: growth (inferred from mutant phenotype from WormBase).
GO:0002119;	Biological process: nematode larval development (inferred from mutant phenotype from WormBase).
GO:0009117;	Biological process: nucleotide metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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.

Genome annotation databases

Ensembl

F32D1.5; Caenorhabditis elegans. [Contig view]

GeneID

178834; -.

KEGG

cel:F32D1.5; -.

Other

902748; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Metal-binding; NADP; Oxidoreductase; Potassium.

Features

Feature table viewer

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