NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=301 / Serotype 2a;
DOI=10.1093/nar/gkf566; PubMed=12384590 [NCBI, ExPASy, EBI, Israel, Japan]
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157.";
Nucleic Acids Res. 30:4432-4441(2002).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700930 / 2457T / Serotype 2a;
DOI=10.1128/IAI.71.5.2775-2786.2003; PubMed=12704152 [NCBI, ExPASy, EBI, Israel, Japan]
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T.";
Infect. Immun. 71:2775-2786(2003).

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.
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

AE005674; AAN41766.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014073; AAP15647.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_706059.1; -.
NP_835842.1; -.

3D structure databases

HSSP

P49058; 1EEP. [HSSP ENTRY / PDB]

ModBase

Q83SM9.

Enzyme and pathway databases

BioCyc

SFLE198214:AAN41766.1-MON; -.

Ontologies

GO:0003920;	Molecular function: GMP reductase activity (inferred from electronic annotation from HAMAP).
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.

BLOCKS

Q83SM9.

Genome annotation databases

GeneID

1024535; -.
1076533; -.

GenomeReviews

AE014073_GR; S0103.
AE005674_GR; SF0101.

KEGG

sfl:SF0101; -.
sfx:S0103; -.

Phylogenomic databases

HOGENOM

Q83SM9; -.

Genome annotation databases

CMR

Q83SM9; SF0101.

Other

ProtoNet

Q83SM9.

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_0000093740`
`NP_BIND`	`108 131`	`24`	`NADP (By similarity).`
`NP_BIND`	`216 239`	`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).`

Sequence information

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

Molecular weight: 37384 Da [This is the MW of the unprocessed precursor]

CRC64: F7C919837982EB40 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRIEEDLKLG FKDVLIRPKR STLKSRSDVE LERQFTFKHS GQSWSGVPII AANMDTVGTF 

        70         80         90        100        110        120 
SMASALASFD ILTAVHKHFS VEEWQAFINN SSADVLKHVM VSTGTSDADF EKTKQILDLN 

       130        140        150        160        170        180 
PALNFVCIDV ANGYSEHFVQ FVAKAREAWP TKTICAGNVV TGEMCEELIL SGADIVKVGI 

       190        200        210        220        230        240 
GPGSVCTTRV KTGVGYPQLS AVIECADAAH GLGGMIVSDG GCTTPGDVAK AFGGGADFVM 

       250        260        270        280        290        300 
LGGMLAGHEE SGGRIVEENG EKFMLFYGMS SESAMKRHVG GVAEYRAAEG KTVKLPLRGQ 

       310        320        330        340 
VENTARDILG GLRSACTYVG ASRLKELTKR TTFIRVLEQE NRIFNNL

Q83SM9 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