NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1128/IAI.68.6.3491-3501.2000; PubMed=10816503 [NCBI, ExPASy, EBI, Israel, Japan]
Lizotte-Waniewski M., Tawe W., Guiliano D.B., Lu W., Liu J., Williams S.A., Lustigman S.;
"Identification of potential vaccine and drug target candidates by expressed sequence tag analysis and immunoscreening of Onchocerca volvulus larval cDNA libraries.";
Infect. Immun. 68:3491-3501(2000).

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

AF153721; AAF64252.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P12268; 1B3O. [HSSP ENTRY / PDB]

ModBase

Q9NJD8.

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`	`1 364`	`364`	`GMP reductase.`	`PRO_0000093730`
`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: 364 AA [This is the length of the unprocessed precursor]

Molecular weight: 39874 Da [This is the MW of the unprocessed precursor]

CRC64: 64224E6F9B14847A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPTIENEPKL DFKDVLLRPK RSTLKSRADV DLVREFVFRN SKKKYVGIPI VASNMDTVGT 

        70         80         90        100        110        120 
FEVAESLSKK RLFTTIHKHY SVDQWMEFVN RISSNQDILS QIGISSGISD YDFTKLKKIC 

       130        140        150        160        170        180 
GLIPELQYIC LDVANGYSEV FVDFIRRVRE EFPRHTIFAG NVVTGEMTEE LILSGADVVK 

       190        200        210        220        230        240 
VGIGSGSVCT TRKKAGVGYP QLSAVLECAD ASHGLNGHVM SDGGCTNPGD VAKALGAGAD 

       250        260        270        280        290        300 
FVMIGGLFAG HDQCGGDTVE KDGQKYKLFY GMSSDTAMEK HEGSVAEYRA SEGKTITVPY 

       310        320        330        340        350        360 
RGDISKTVQD LLGGLRSACT YTGAKKLKEL SKRATFVRVT QQTNEQYATF EISPSELQNL 


NIAV

Q9NJD8 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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