Reviewed, UniProtKB/Swiss-Prot P27442 (GMPR_ASCSU)

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	Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Taxonomic identifier	6253 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Nematoda › Chromadorea › Ascaridida › Ascaridoidea › Ascarididae › Ascaris

Protein attributes

Sequence length	356 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.
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 – 356	356	GMP reductase		PRO_0000093728
Regions
	Nucleotide binding	111 – 134	24	NADP By similarity
Sites
	Active site	189	1	Thioimidate intermediate By similarity
	Metal binding	184	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	186	1	Potassium; via carbonyl oxygen By similarity
	Binding site	222	1	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P27442-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 2D1B4F1B64EFB26A	FASTA	356	39,252
	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

References

[1]	"The GMP reductase gene of the nematode Ascaris lumbricoides var. suum." Gruidl M.E., Bunch K., Gharib S., Bennett K.L. Mol. Biochem. Parasitol. 52:271-274(1992) [PubMed: 1620164] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	M82838 mRNA. Translation: AAA29373.1.
3D structure databases
HSSP	HSSP built from PDB template 1B3O based on UniProtKB P12268.
SMR	P27442. Positions 10-340.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.7.1.7. 649.
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_ASCSU

Accession

Primary (citable) accession number: P27442

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)