Reviewed, UniProtKB/Swiss-Prot P59075 (GMPR_PHYIN)

Names and origin

Protein names	Recommended name:     GMP reductase     EC=1.7.1.7 Alternative name(s):     Guanosine 5'-monophosphate oxidoreductase       Short name=Guanosine monophosphate reductase
Organism	Phytophthora infestans (Potato late blight fungus)
Taxonomic identifier	4787 [NCBI]
Taxonomic lineage	Eukaryota › stramenopiles › Oomycetes › Peronosporales › Phytophthora

Protein attributes

Sequence length	362 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (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.
Sequence similarities	Belongs to the IMPDH/GMPR family.

Ontologies

Keywords
Ligand	Metal-binding NADP Potassium
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	nucleotide metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	GMP reductase activity Inferred from electronic annotation. Source: EC potassium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 362	362	GMP reductase		PRO_0000093731
Regions
	Nucleotide binding	108 – 131	24	NADP By similarity
Sites
	Active site	186	1	Thioimidate intermediate By similarity
	Metal binding	181	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	183	1	Potassium; via carbonyl oxygen By similarity
	Binding site	219	1	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P59075-1 [UniParc]. Last modified November 8, 2002. Version 1. Checksum: C15F5F041372F5EC	FASTA	362	38,924
	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

References

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF424648 mRNA. Translation: AAN31473.1.
3D structure databases
HSSP	HSSP built from PDB template 1EEP based on UniProtKB P49058.
SMR	P59075. Positions 10-336.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.7.1.7. 81513.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR005993. GMP_reduct1. IPR015875. IMP_DH/GMP_Rdtase_CS. IPR001093. IMP_DH_GMPRt. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF00478. IMPDH. 1 hit. [Graphical view]
PIRSF	PIRSF000235. GMP_reductase. 1 hit.
TIGRFAMs	TIGR01305. GMP_reduct_1. 1 hit.
PROSITE	PS00487. IMP_DH_GMP_RED. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GMPR_PHYIN

Accession

Primary (citable) accession number: P59075

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	November 8, 2002
Last modified:	June 16, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)