NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tomasz A., Richardson P.;
"Complete sequence of chromosome of Staphylococcus aureus subsp. aureus JH9.";
Submitted (MAY-2007) 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. GuaC type 2 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

CP000703; ABQ49192.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001246768.1; -.

3D structure databases

ModBase

A5ISL9.

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_01511; -; 1.
PBIL [Tree]

InterPro

IPR005994; GMP_reduct2.
IPR015875; IMP_DH/GMP_Rdtase_CS.
IPR001093; IMP_DHase_GMPRtase.
Graphical view of domain structure.

Pfam

PF00478; IMPDH; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF036500; GMP_red_Firmic; 1.

TIGRFAMs

TIGR01306; GMP_reduct_2; 1.

PROSITE

PS00487; IMP_DH_GMP_RED; 1.

Genome annotation databases

GeneID

5168311; -.

GenomeReviews

CP000703_GR; SaurJH9_1398.

KEGG

saj:SaurJH9_1398; -.

CMR

A5ISL9; SaurJH9_1398.

Other

UniRef

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

Keywords

Complete proteome; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 325`	`325`	`GMP reductase.`	`PRO_1000087525`
`NP_BIND`	`203 226`	`24`	`NADP (Potential).`
`ACT_SITE`	`174 174`		`Thioimidate intermediate (By similarity).`

Sequence information

Length: 325 AA [This is the length of the unprocessed precursor]

Molecular weight: 36129 Da [This is the MW of the unprocessed precursor]

CRC64: F8FF7A9D55552BBC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKIFDYEDIQ LIPNKCIVES RSECDTTIQF GPKKFKLPVV PANMQTVMNE KLAKWFAEND 

        70         80         90        100        110        120 
YFYIMHRFDE EARIPFIKHM QNSGLFASIS VGVKKAEFDF IEKLAQEKLI PEYITIDIAH 

       130        140        150        160        170        180 
GHSDSVINMI KHIKNHIPDS FVIAGNVGTP EGVRELENAG ADATKVGIGP GRVCITKIKT 

       190        200        210        220        230        240 
GFGTGGWQLA ALNICSKAAR KPLIADGGIR THGDIAKSIR FGASMVMIGS LFAAHEESPG 

       250        260        270        280        290        300 
ETVELDGKQY KEYFGSASEF QKGEHKNVEG KKMFVEHKGS LMDTLKEMQQ DLQSSISYAG 

       310        320 
GKDLKSLRTV DYVIVRNSIF NGDRD

A5ISL9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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