B7LWQ6 (GUAC_ESCF3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GMP reductase
EC=1.7.1.7

Alternative name(s):
Guanosine 5'-monophosphate oxidoreductase
Short name=Guanosine monophosphate reductase

Gene names

Name:	guaC
Ordered Locus Names:	EFER_0125

Organism

Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73) [Complete proteome] [HAMAP]

Taxonomic identifier

585054 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	347 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (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. HAMAP MF_00596
Catalytic activity	Inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH. HAMAP MF_00596
Subunit structure	Homotetramer By similarity. HAMAP MF_00596
Sequence similarities	Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.

Ontologies

Keywords
Ligand	Metal-binding NADP Potassium
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	nucleotide metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	GMP reductase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 347	347	GMP reductase HAMAP MF_00596		PRO_1000129858
Regions
	Nucleotide binding	108 – 131	24	NADP By similarity
	Nucleotide binding	216 – 239	24	NADP; ribose moiety By similarity
Sites
	Active site	186	1	Thioimidate intermediate By similarity
	Metal binding	181	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	183	1	Potassium; via carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7LWQ6 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: F9836F18CAED998E	FASTA	347	37,285
	10 20 30 40 50 60 MRIEEDLKLG FKDVLIRPKR STLKSRSDVE LERQFTFKHS GQSWSGVPII AANMDTVGTF 70 80 90 100 110 120 SMASALASFD ILTAVHKHYS VEEWLAFVNS SSVDVLKHVM VSTGTSDADF EKTKQILALN 130 140 150 160 170 180 PALNFVCIDV ANGYSEHFVQ FVAKAREAWP TKTICAGNVV TGEMCEELIL SGADIVKVGI 190 200 210 220 230 240 GPGSVCTTRV KTGVGYPQLS AVIECADAAH GLGGMIVSDG GCTTPGDVAK AFGGGADFVM 250 260 270 280 290 300 LGGMLAGHEE SGGRIVEENG EKFMLFYGMS SESAMKRHVG GVAEYRAAEG KTVKLPLRGP 310 320 330 340 VENTARDILG GLRSACTYVG ASRLKELTKR TTFIRVQEQE NRIFNSL

References

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed: 19165319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35469 / DSM 13698 / CDC 0568-73.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928158 Genomic DNA. Translation: CAQ87708.1.
RefSeq	YP_002381351.1. NC_011740.1.
3D structure databases
ProteinModelPortal	B7LWQ6.
ModBase	Search...
Protein-protein interaction databases
STRING	B7LWQ6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000122212; EBESCP00000115015; EBESCG00000123809.
GeneID	7120910.
GenomeReviews	Gene locus EFER_0125 in contig CU928158_GR.
KEGG	efe:EFER_0125.
PATRIC	32124685. VBIEscFer122920_0131.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000009443.
HOGENOM	HBG298985.
ProtClustDB	PRK05096.
Enzyme and pathway databases
BioCyc	EFER585054:EFER_0125-MONOMER.
Family and domain databases
HAMAP	MF_00596. GMP_reduct_type1. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR005993. GMP_reduct1. IPR015875. IMP_DH/GMP_Rdtase_CS. IPR001093. IMP_DH_GMPRt. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K00364.
PANTHER	PTHR11911:SF33. PTHR11911:SF33. 1 hit.
Pfam	PF00478. IMPDH. 1 hit. [Graphical view]
PIRSF	PIRSF000235. GMP_reductase. 1 hit.
TIGRFAMs	TIGR01305. GMP_reduct_1. 1 hit.
PROSITE	PS00487. IMP_DH_GMP_RED. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUAC_ESCF3

Accession

Primary (citable) accession number: B7LWQ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 10, 2009
Last modified:	January 25, 2012
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program