NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nbt1325; PubMed=17704766 [NCBI, ExPASy, EBI, Israel, Japan]
Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R.;
"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42.";
Nat. Biotechnol. 25:1007-1014(2007).

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

CP000560; ABS75249.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001422480.1; -.

3D structure databases

ModBase

A7Z8C3.

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

IPR013785; Aldolase_TIM.
IPR005994; GMP_reduct2.
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

PIRSF036500; GMP_red_Firmic; 1.

TIGRFAMs

TIGR01306; GMP_reduct_2; 1.

PROSITE

PS00487; IMP_DH_GMP_RED; 1.

BLOCKS

A7Z8C3.

Genome annotation databases

GeneID

5460081; -.

GenomeReviews

CP000560_GR; RBAM_029180.

KEGG

bay:RBAM_029180; -.

CMR

A7Z8C3; RBAM_029180.

Other

ProtoNet

A7Z8C3.

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`	`1 326`	`326`	`GMP reductase.`	`PRO_1000024490`
`NP_BIND`	`204 227`	`24`	`NADP (Potential).`
`ACT_SITE`	`175 175`		`Thioimidate intermediate (By similarity).`

Sequence information

Length: 326 AA [This is the length of the unprocessed precursor]

Molecular weight: 35852 Da [This is the MW of the unprocessed precursor]

CRC64: A2FD907375378B9A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MENVFDYEDI QLIPAKCIVD SRSECDTSVT LGGHTFKLPV VPANMQTIID ENIAAWLAEN 

        70         80         90        100        110        120 
GYFYIMHRFE PEKRLAFVQD MKARGLISSI SVGVKENDYE FIRELKAQEL VPDYITIDIA 

       130        140        150        160        170        180 
HGHSNAVISM IQFIKEHVPE SFVIAGNVGT PEAVRELERA GADATKVGIG PGKVCITKIK 

       190        200        210        220        230        240 
TGFGTGGWQL AALRWCAKAA SKPIIADGGI RTHGDIAKSI RFGASMVMIG SLFAGHEESP 

       250        260        270        280        290        300 
GQTIEIDGKL YKEYFGSASE FQKGEKKNVE GKKMHVEHKG SLQDTLVEME QDLQSSISYA 

       310        320 
GGNTLEAIRN VDYVIVKNSI FNGDRF

A7Z8C3 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