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., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
"Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
Submitted (FEB-2006) 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

CP000267; ABD70748.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_524279.1; -.

3D structure databases

ModBase

Q21U05.

Enzyme and pathway databases

BioCyc

RFER338969:RFER_3037-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_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

Q21U05.

Genome annotation databases

GeneID

3961012; -.

GenomeReviews

CP000267_GR; Rfer_3037.

KEGG

rfr:Rfer_3037; -.

NMPDR

fig|338969.3.peg.3457; -.

Phylogenomic databases

HOGENOM

Q21U05; -.

Genome annotation databases

CMR

Q21U05; Rfer_3037.

Other

ProtoNet

Q21U05.

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_0000294283`
`NP_BIND`	`202 225`	`24`	`NADP (Potential).`
`ACT_SITE`	`173 173`		`Thioimidate intermediate (By similarity).`

Sequence information

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

Molecular weight: 35813 Da [This is the MW of the unprocessed precursor]

CRC64: 0DBB4DB4564FB50D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEIFDYDNIL LLPRKCRVES RSECDASVEL GRQRFRIPVV PANMKTVVDE SICVWLAQNS 

        70         80         90        100        110        120 
YFYVMHRFDL DNVQFVKNMK ARGLYASISL GVKKPDYDTV DQLLALGLVP DYITIDIAHG 

       130        140        150        160        170        180 
HADSVKNMIG YLKEKMPTVF IIAGNVATPE AVIDLENWGA DATKVGIGPG KVCITKLKTG 

       190        200        210        220        230        240 
FGTGGWQLSA VKWCARVATK PIIADGGIHE HGDIAKSIRF GATMVMIGSM LAGHEESPGK 

       250        260        270        280        290        300 
SVEVDGKLYK EYYGSASDFN KGEYKHVEGK RILEPVKGKL ADTLIEMEQD VQSSISYSGG 

       310        320 
KRLMDIRKVN YVTLGGDNAG EHLLM

Q21U05 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