[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=DDR7602; Torto T.A., Styer A., Kamoun S.; "EST mining and functional expression assays identify extracellular elicitor proteins from Phytophthora."; Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.

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

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Cross-references

Sequence databases

EMBL

AF424648; AAN31473.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P49058; 1EEP. [HSSP ENTRY / PDB]

SMR

P59075; 10-336.

ModBase

P59075.

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`	`1 362`	`362`	`GMP reductase.`	`PRO_0000093731`
`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).`

Sequence information

Length: 362 AA [This is the length of the unprocessed precursor]

Molecular weight: 38924 Da [This is the MW of the unprocessed precursor]

CRC64: C15F5F041372F5EC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPRIETEVRL DFKDVLIRPK RSTLKSRSQV DVQREFRFLN SKRTWSGVPV IAANMDTVGT 

        70         80         90        100        110        120 
FEMAVELAKL EFITCVHKHY TPQDWATFAA KHPDVLPTVA VSGGSSAADV EKITAILKSH 

       130        140        150        160        170        180 
PDIRFICLDV ANGYSEVFVQ AVRNVRSAFP EHTIIAGNVV TGEMVEELLL SGADIIKVGI 

       190        200        210        220        230        240 
GPGSVCTTRK QTGVGYPQLS AVLECADAAH GLNGHVISDG GCTCPGDVAK AFGAGADFVM 

       250        260        270        280        290        300 
LGGMLAGHDE SGGDKIEING KLLKKFYGMS SSEAMKKHNG GVAEYRASEG KSVTVPYRGP 

       310        320        330        340        350        360 
VSGTCKEILG GVRSTCTYVG ASKLKEISKR TTFIRVSQQL NEVFGRAPNE QEEQVSKKQK 


TG

P59075 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