P0A8Y2 (YJJG_ECO57) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyrimidine 5'-nucleotidase YjjG
EC=3.1.3.5

Alternative name(s):
House-cleaning nucleotidase
Non-canonical pyrimidine nucleotide phosphatase
Nucleoside 5'-monophosphate phosphohydrolase
dUMP phosphatase

Gene names

Name:	yjjG
Ordered Locus Names:	Z5975, ECs5332

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	225 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Nucleotidase that shows high phosphatase activity toward non-canonical pyrimidine nucleotides and three canonical nucleoside 5'-monophosphates (UMP, dUMP, and dTMP), and very low activity against TDP, IMP, UDP, GMP, dGMP, AMP, dAMP, and 6-phosphogluconate. Appears to function as a house-cleaning nucleotidase in vivo, since the general nucleotidase activity of YjjG allows it to protect cells against non-canonical pyrimidine derivatives such as 5-fluoro-2'-deoxyuridine, 5-fluorouridine, 5-fluoroorotate, 5-fluorouracil, and 5-aza-2'-deoxycytidine, and prevents the incorporation of potentially mutagenic nucleotides into DNA. Its dUMP phosphatase activity that catalyzes the hydrolysis of dUMP to deoxyuridine is necessary for thymine utilization via the thymine salvage pathway. Is strictly specific to substrates with 5'-phosphates and shows no activity against nucleoside 2'- or 3'-monophosphates By similarity.
Catalytic activity	A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Cofactor	Divalent metal cation. Manganese or magnesium By similarity.
Subcellular location	Cytoplasm Potential.
Sequence similarities	Belongs to the HAD-like hydrolase superfamily. YjjG family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	5'-nucleotidase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoglycolate phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 225	225	Pyrimidine 5'-nucleotidase YjjG		PRO_0000066273
Sites
	Active site	9	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A8Y2 [UniParc]. Last modified June 21, 2005. Version 1. Checksum: D8A52E086567BA71	FASTA	225	25,301
	10 20 30 40 50 60 MKWDWIFFDA DETLFTFDSF TGLQRMFLDY SVTFTAEDFQ DYQAVNKPLW VDYQNGAITS 70 80 90 100 110 120 LQLQHGRFES WAERLNVEPG KLNEAFINAM AEICTPLPGA VSLLNAIRGN AKIGIITNGF 130 140 150 160 170 180 SALQQVRLER TGLRDYFDLL VISEEVGVAK PNKKIFDYAL EQAGNPDRSR VLMVGDTAES 190 200 210 220 DILGGINAGL ATCWLNAHHR EQPEGIAPTW TVSSLHELEQ LLCKH

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG59554.1. BA000007 Genomic DNA. Translation: BAB38755.1.
PIR	D91295. F86136.
RefSeq	NP_290987.1. NC_002655.2. NP_313359.1. NC_002695.1.
3D structure databases
ProteinModelPortal	P0A8Y2.
SMR	P0A8Y2. Positions 1-222.
ModBase	Search...
Protein-protein interaction databases
STRING	155864.Z5975.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAG59554; AAG59554; Z5975. BAB38755; BAB38755; BAB38755.
GeneID	913547. 959681.
KEGG	ece:Z5975. ecs:ECs5332.
PATRIC	18360320. VBIEscCol44059_5290.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1011.
HOGENOM	HOG000248345.
KO	K08723.
OMA	ICAPLPG.
ProtClustDB	PRK09449.
Enzyme and pathway databases
BioCyc	ECOL386585:GJFA-5345-MONOMER.
Family and domain databases
Gene3D	1.10.150.240. 1 hit. 3.40.50.1000. 1 hit.
InterPro	IPR023214. HAD-like_dom. IPR006439. HAD-SF_hydro_IA_v1. IPR006402. HAD-SF_hydro_IA_v3. IPR011951. HAD-SF_hydro_IA_YjjG/YfnB. IPR023198. PGP_dom2. [Graphical view]
Pfam	PF00702. Hydrolase. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01549. HAD-SF-IA-v1. 1 hit. TIGR01509. HAD-SF-IA-v3. 1 hit. TIGR02254. YjjG/YfnB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

YJJG_ECO57

Accession

Primary (citable) accession number: P0A8Y2
Secondary accession number(s): P33999, P76818

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	June 21, 2005
Last modified:	May 1, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program