NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nbt1160; PubMed=16273110 [NCBI, ExPASy, EBI, Israel, Japan]
Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M., Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., Loux V., Zagorec M.;
"The complete genome sequence of the meat-borne lactic acid bacterium Lactobacillus sakei 23K.";
Nat. Biotechnol. 23:1527-1533(2005).

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

CR936503; CAI54777.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_395089.1; -.

3D structure databases

SMR

Q38YF0; 2-319.

ModBase

Q38YF0.

Enzyme and pathway databases

BioCyc

LSAK314315:LSA0476-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

Q38YF0.

Genome annotation databases

GeneID

3777651; -.

GenomeReviews

CR936503_GR; LSA0476.

KEGG

lsa:LSA0476; -.

Phylogenomic databases

HOGENOM

Q38YF0; -.

Genome annotation databases

CMR

Q38YF0; LSA0476.

Other

ProtoNet

Q38YF0.

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_0000292052`
`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: 36067 Da [This is the MW of the unprocessed precursor]

CRC64: FC050439A34AA543 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDVFDYEDVQ LIPNKCIVKS RSEIDTTVRF GSETFKIPVV PANMQTIIDE PLAIWLAENH 

        70         80         90        100        110        120 
YFYVMHRFQP EKRPAFIKMM HERNLFASIS VGVKDDEFDF INQLAQDNLI PEYITIDIAH 

       130        140        150        160        170        180 
GHSQVVIDMI QHIKKVLPKS FVIAGNVGTP EAVRDLERAG ADATKVGIGP GKVCITKIKT 

       190        200        210        220        230        240 
GFGTGGWQLG ALRWCAKAAT KPIIADGGIR TNGDIAKSIR FGANMVMIGS LFAGHTESPG 

       250        260        270        280        290        300 
ELVEEDGQQF KEYFGSASEF QKGTHQNVEG KRILVPYKGS ISDTLTEMRQ DLQSSISYAG 

       310        320 
GKRLSALRKV DYVLVRHSIF NGDML

Q38YF0 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