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.
SUBUNIT: Homotetramer (By similarity).
SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.

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

CP000826; ABV39881.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001477009.1; -.

3D structure databases

ModBase

A8G9U1.

Ontologies

GO:0003920;	Molecular function: GMP reductase activity (inferred from electronic annotation from HAMAP).
GO:0030955;	Molecular function: potassium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006163;	Biological process: purine nucleotide metabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00596; -; 1.
PBIL [Tree]

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.

Genome annotation databases

GeneID

5604325; -.

GenomeReviews

CP000826_GR; Spro_0775.

KEGG

spe:Spro_0775; -.

CMR

A8G9U1; Spro_0775.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Metal-binding; NADP; Oxidoreductase; Potassium.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 347`	`347`	`GMP reductase.`	`PRO_1000061238`
`NP_BIND`	`108 131`	`24`	`NADP (By similarity).`
`NP_BIND`	`216 239`	`24`	`NADP; ribose moiety (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).`

Sequence information

Length: 347 AA [This is the length of the unprocessed precursor]

Molecular weight: 37301 Da [This is the MW of the unprocessed precursor]

CRC64: 7F2CE91770EC5754 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRIEEDLKLG FKDVLIRPKR STLKSRSEVE LERQFTFKHS GLSWSGVPII AANMDSVGTF 

        70         80         90        100        110        120 
SMAEALASFD VLTAVHKHYT LEQWAAFVQR VPASVLRHVM VSTGTSEADF VKMQQILALS 

       130        140        150        160        170        180 
PGLKFICIDV ANGYSEHFVA FLQKAREACP NHVICAGNVV TGEMVEELIL SGADIVKVGI 

       190        200        210        220        230        240 
GPGSVCTTRV KTGVGYPQLS AVIECADAAH GLGGQIVSDG GCSVPGDVAK AFGGGADFVM 

       250        260        270        280        290        300 
LGGMLAGHDE CEGTVVEENG EKFMLFYGMS SESAMKRHVG GVAQYRAAEG KTVKLPLRGE 

       310        320        330        340 
VEFTVRDILG GLRSACTYVG AERLKELTKR TTFIRVAEQE NRVFGSN

A8G9U1 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