[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

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

BC003886; AAH03886.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC024109; AAH24109.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

UniGene

Mm.390685

3D structure databases

HSSP

P49058; 1EEP. [HSSP ENTRY / PDB]

SMR

Q99L27; 10-337.

ModBase

Q99L27.

Organism-specific databases

MGI

MGI:1917903; Gmpr2.

Gene expression databases

CleanEx

MM_GMPR2; -.

GermOnline

ENSMUSG00000002326; Mus musculus.

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

Q99L27.

Genome annotation databases

Ensembl

ENSMUSG00000002326; Mus musculus. [Contig view]

Phylogenomic databases

HOGENOM

Q99L27; -.

HOVERGEN

Q99L27; -.

Other

Gmpr2; Mus musculus.

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

Keywords

Metal-binding; NADP; Oxidoreductase; Potassium.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 348`	`348`	`GMP reductase 2.`	`PRO_0000093727`
`NP_BIND`	`108 131`	`24`	`NADP (By similarity).`
`ACT_SITE`	`186 186`		`Thioimidate intermediate (By similarity).`
`METAL`	`181 181`		`Potassium; via carbonyl oxygen (By similarity).`
`METAL`	`183 183`		`Potassium; via carbonyl oxygen (By similarity).`
`BINDING`	`219 219`		`NADP (By similarity).`
`CONFLICT`	`105 105`		`T -> S (in Ref. 1; AAH24109).`

Sequence information

Length: 348 AA [This is the length of the unprocessed precursor]

Molecular weight: 38033 Da [This is the MW of the unprocessed precursor]

CRC64: 83E69980D6877A97 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPHIDNDVKL DFKDVLLRPK RSTLKSRSEV ELTRSFSFRN SKQMYSGIPV IAANMDTVGT 

        70         80         90        100        110        120 
FEMARVLCKF SLFTAIHKHY SIHQWQEFAS QNPDCLECLA ASSGTGSADF EQLEQILEAI 

       130        140        150        160        170        180 
PQVKYICLDV ANGYSEHFVE FVKDVRKRFP QHTIMAGNVV TGEMVEELIL SGADIIKVGI 

       190        200        210        220        230        240 
GPGSVCTTRK KTGVGYPQLS AVMECADAAH GLKGHIISDG GCSCPGDVAK AFGAGADFVM 

       250        260        270        280        290        300 
LGGMLAGHSE SGGELIERDG KKYKLFYGMS SEMAMKKYSG GVAEYRASEG KIVEVPFKGD 

       310        320        330        340 
VEHTIRDILG GIRSTCTYVG AAKLKELSRR TTFIRVTQQV NPIFSNSQ

Q99L27 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