P33025 (PSUG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pseudouridine-5'-phosphate glycosidase
Short name=PsiMP glycosidase
EC=3.2.-.-

Gene names

Name:	psuG
Synonyms:	yeiN
Ordered Locus Names:	b2165, JW2152

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the hydrolysis of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. In vitro, can also catalyze the reverse reaction. Ref.4
Catalytic activity	Pseudouridine 5'-phosphate + H2O = uracil + D-ribose 5-phosphate. Ref.4
Cofactor	Divalent metal cations. Active with Fe2+, Co2+ and Mn2+, whereas Zn2+ and Ni2+ are inhibitors. Ref.4
Sequence similarities	Belongs to the pseudouridine-5'-phosphate glycosidase family.
Biophysicochemical properties	Kinetic parameters: KM=60 µM for pseudouridine 5'-phosphate (in the presence of 0.5 mM Mn2+) Ref.4

Ontologies

Keywords
Ligand	Metal-binding
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	hydrolase activity, acting on glycosyl bonds Inferred from electronic annotation. Source: UniProtKB-KW 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 – 312	312	Pseudouridine-5'-phosphate glycosidase HAMAP MF_01876		PRO_0000169150

Sequences

	Sequence		Length	Mass (Da)
	P33025 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: EBD892C271404F1F	FASTA	312	32,910
	10 20 30 40 50 60 MSELKISPEL LQISPEVQDA LKNKKPVVAL ESTIISHGMP FPQNAQTAIE VEETIRKQGA 70 80 90 100 110 120 VPATIAIIGG VMKVGLSKEE IELLGREGHN VTKVSRRDLP FVVAAGKNGA TTVASTMIIA 130 140 150 160 170 180 ALAGIKVFAT GGIGGVHRGA EHTFDISADL QELANTNVTV VCAGAKSILD LGLTTEYLET 190 200 210 220 230 240 FGVPLIGYQT KALPAFFCRT SPFDVSIRLD SASEIARAMV VKWQSGLNGG LVVANPIPEQ 250 260 270 280 290 300 FAMPEHTINA AIDQAVAEAE AQGVIGKEST PFLLARVAEL TGGDSLKSNI QLVFNNAILA 310 SEIAKEYQRL AG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Automated multiplex sequencing of the E.coli genome." Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M. Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / BHB2600.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Molecular identification of pseudouridine-metabolizing enzymes." Preumont A., Snoussi K., Stroobant V., Collet J.-F., Van Schaftingen E. J. Biol. Chem. 283:25238-25246(2008) [PubMed: 18591240] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. Strain: K12.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00007 Genomic DNA. Translation: AAA60517.1. U00096 Genomic DNA. Translation: AAC75226.1. AP009048 Genomic DNA. Translation: BAE76642.1.
PIR	D64985.
RefSeq	NP_416670.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P33025.
SMR	P33025. Positions 10-309.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-11926N.
IntAct	P33025. 13 interactions.
MINT	MINT-1308217.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000000398; EBESCP00000000398; EBESCG00000000328. EBESCT00000016423; EBESCP00000015714; EBESCG00000015483.
GeneID	946699.
GenomeReviews	Gene locus JW2152 in contig AP009048_GR. Gene locus b2165 in contig U00096_GR.
KEGG	ecj:JW2152. eco:b2165.
PATRIC	32119679. VBIEscCol129921_2250.
Organism-specific databases
EchoBASE	EB1968.
EcoGene	EG12033. psuG.
Phylogenomic databases
eggNOG	COG2313.
GeneTree	EBGT00050000010754.
HOGENOM	HBG308892.
OMA	PATIAVM.
PhylomeDB	P33025.
ProtClustDB	CLSK862888.
Enzyme and pathway databases
BioCyc	EcoCyc:EG12033-MONOMER.
Gene expression databases
Genevestigator	P33025.
Family and domain databases
HAMAP	MF_01876. PsiMP_glycosidase. [Tree]
InterPro	IPR022830. Indigdn_synthA-like. IPR007342. PseudoU_P_glycosidase. [Graphical view]
Pfam	PF04227. Indigoidine_A. 1 hit. [Graphical view]
SUPFAM	SSF110581. Indigdn_synthA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PSUG_ECOLI

Accession

Primary (citable) accession number: P33025
Secondary accession number(s): Q2MAR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	January 25, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program