NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IL1403;
DOI=10.1101/gr.GR-1697R; PubMed=11337471 [NCBI, ExPASy, EBI, Israel, Japan]
Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A.;
"The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403.";
Genome Res. 11:731-753(2001).

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

AE006347; AAK05243.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A86768; A86768.

RefSeq

NP_267301.1; -.

3D structure databases

HSSP

P12268; 1B3O. [HSSP ENTRY / PDB]

SMR

Q9CGF1; 4-324.

ModBase

Q9CGF1.

Enzyme and pathway databases

BioCyc

LLAC272623:L158186-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

Q9CGF1.

Genome annotation databases

1114786; -.

AE005176_GR; LL1145.

lla:L158186; -.

fig|272623.1.peg.1178; -.

Phylogenomic databases

HOGENOM

Q9CGF1; -.

Genome annotation databases

CMR

Q9CGF1; LL1145.

Other

ProtoNet

Q9CGF1.

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`	`1 329`	`329`	`GMP reductase.`	`PRO_0000093761`
`NP_BIND`	`207 230`	`24`	`NADP (By similarity).`
`ACT_SITE`	`178 178`		`Thioimidate intermediate (By similarity).`

Sequence information

Length: 329 AA [This is the length of the unprocessed precursor]

Molecular weight: 35837 Da [This is the MW of the unprocessed precursor]

CRC64: 187BDCC3564FDA17 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNNLNSVFDY EDIQLIPNKC VINSRLEADT SVKLGNFTFK LPVVPANMQT IIDDKIAEML 

        70         80         90        100        110        120 
AKEGYFYIMH RFEAENRAAF IKKMHQQGLI ASISVGVKAD EHAFIREISA DALIPEFITI 

       130        140        150        160        170        180 
DIAHGHADSV IKTIQLIKRL MPQTFVIAGN VGTPEAVREL ENAGADATKV GIGPGKVCIT 

       190        200        210        220        230        240 
KVKTGFGTGG WQLAAVKWCA KAASKPVIAD GGIRTHGDIA KSIRMGATMV MVGSLFAAHE 

       250        260        270        280        290        300 
ESPGQTVERD GQLFKEYFGS ASEYQKGEHK NVEGKKILLP HKGSLKDTLK EMEEDLQSSI 

       310        320 
SYAGGRDLSA LTKVDYVVVK NSIWNGDAI

Q9CGF1 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