[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0166-6851(92)90059-S; PubMed=1620164 [NCBI, ExPASy, EBI, Israel, Japan] Gruidl M.E., Bunch K., Gharib S., Bennett K.L.; "The GMP reductase gene of the nematode Ascaris lumbricoides var. suum."; Mol. Biochem. Parasitol. 52:271-274(1992).

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.
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

M82838; AAA29373.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P12268; 1B3O. [HSSP ENTRY / PDB]

SMR

P27442; 10-340.

ModBase

P27442.

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: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.

Other

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`	`1 356`	`356`	`GMP reductase.`	`PRO_0000093728`
`NP_BIND`	`111 134`	`24`	`NADP (By similarity).`
`ACT_SITE`	`189 189`		`Thioimidate intermediate (By similarity).`
`METAL`	`184 184`		`Potassium; via carbonyl oxygen (By similarity).`
`METAL`	`186 186`		`Potassium; via carbonyl oxygen (By similarity).`
`BINDING`	`222 222`		`NADP (By similarity).`

Sequence information

Length: 356 AA [This is the length of the unprocessed precursor]

Molecular weight: 39252 Da [This is the MW of the unprocessed precursor]

CRC64: 2D1B4F1B64EFB26A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPRIEFEPKL DFKDVLLRPK RSTLRSRAEV DLMREYVFRN SKKTYVGVPV VASNMDTVGT 

        70         80         90        100        110        120 
FEMAEVLAKF SLFTTIHKHY QVDEWKAFVQ RVDSNPQIMS QIGISSGIST SDFDKLRTVC 

       130        140        150        160        170        180 
DMIPELEYIC LDVANGYSEV FVDFIRRVRE QFPTHTIFAG NVVTGEMVEE LILSGADVVK 

       190        200        210        220        230        240 
VGIGPGSVCT TRKKAGVGYP QLSAVLECAD ASHGLNGHVM SDGGCTNPGD VAKAFGGGAD 

       250        260        270        280        290        300 
FVMIGGLLAG HDQCGGEVVE KDGKKYKLFY GMSSDTAMKK YQGSVAEYRA SEGKTIYMPY 

       310        320        330        340        350 
RGDVSRTIHD LLGGLRSACT YIGATKLKEL SKRATFVRVT QQTNDQYSAY EVPRID

P27442 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