NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33453 / L1 / NBRC 100688 / NCTC 11704;
Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S., Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
Submitted (JUN-2004) 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

AE017263; AAT75527.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_053411.1; -.

3D structure databases

ModBase

Q6F1U6.

Enzyme and pathway databases

BioCyc

MFLO265311:MFL170-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

Q6F1U6.

Genome annotation databases

GeneID

2898130; -.

GenomeReviews

AE017263_GR; Mfl170.

KEGG

mfl:Mfl170; -.

Phylogenomic databases

HOGENOM

Q6F1U6; -.

Genome annotation databases

CMR

Q6F1U6; Mfl170.

Other

ProtoNet

Q6F1U6.

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`	`1 320`	`320`	`GMP reductase.`	`PRO_0000294277`
`NP_BIND`	`203 226`	`24`	`NADP (Potential).`
`ACT_SITE`	`174 174`		`Thioimidate intermediate (By similarity).`

Sequence information

Length: 320 AA [This is the length of the unprocessed precursor]

Molecular weight: 35585 Da [This is the MW of the unprocessed precursor]

CRC64: 53933FE2937D8CCD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYAFDYEDIQ LIPNMCVVNS RSECNTSVTL GKHTFKMPVV PANMATVINE ELSIMLAEKN 

        70         80         90        100        110        120 
YFYVMHRFDF DAVSFIKKMK EKKLISSISV GVKEQDFKMI NELTELNLIP DYITIDIAHG 

       130        140        150        160        170        180 
HANSVKEMIE HIRTKMGDQT FIIAGNVATP QAVRDLEHWG ADATKVGVGP GKVCITKLKT 

       190        200        210        220        230        240 
GFGTGGWQLG AIKWCSKAAT KPIIADGGLR VNGDIAKSIR FGATMCMIGS LFAAHEESPG 

       250        260        270        280        290        300 
KNVTVDNVLF KEYYGSASEY NKGEKRYVEG KKELIKVRGK LMDTYKEMEE DLQSSISYAG 

       310        320 
GKTLKAIKKV DYVILKTSNF

Q6F1U6 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