Q9RN37 (USHA_SALPU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein UshA

Including the following 2 domains:

1. UDP-sugar hydrolase
   EC=3.6.1.45
   Alternative name(s):
   UDP-sugar diphosphatase
   UDP-sugar pyrophosphatase
2. 5'-nucleotidase
   Short name=5'-NT
   EC=3.1.3.5

Gene names

Name:

ushA

Organism

Salmonella pullorum

Taxonomic identifier

605 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I

Protein attributes

Sequence length	550 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell By similarity.
Catalytic activity	UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate. A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Periplasm By similarity.
Sequence similarities	Belongs to the 5'-nucleotidase family.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase
PTM	Disulfide bond
Gene Ontology (GO)
Biological_process	nucleotide catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	5'-nucleotidase activity Inferred from electronic annotation. Source: EC UDP-sugar diphosphatase 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	By similarity
	Chain	26 – 550	525	Protein UshA		PRO_0000000032
Regions
	Region	498 – 504	7	Substrate binding By similarity
Sites
	Metal binding	41	1	Zinc 1 By similarity
	Metal binding	43	1	Zinc 1 By similarity
	Metal binding	84	1	Zinc 1 By similarity
	Metal binding	84	1	Zinc 2 By similarity
	Metal binding	116	1	Zinc 2 By similarity
	Metal binding	217	1	Zinc 2 By similarity
	Metal binding	252	1	Zinc 2 By similarity
	Metal binding	254	1	Zinc 1 By similarity
	Binding site	429	1	Substrate By similarity
	Site	117	1	Transition state stabilizer By similarity
	Site	120	1	Transition state stabilizer By similarity
Amino acid modifications
	Disulfide bond	258 ↔ 275		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9RN37 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 655BC7E8F0D4F62F	FASTA	550	60,604
	10 20 30 40 50 60 MKFLKRGVAL ALLAAFALTT QPAQAYEKDK TYKITILHTN DHHGHFWRSE YGEYGLAAQK 70 80 90 100 110 120 TLVDSIRKEV AQEGGGVLLL SGGDINTGVP ESDLQDAEPD FRGMNLIGYD AMAVGNHEFD 130 140 150 160 170 180 NPLTVLRQQE KWAKFPFLSA NIYQKSTGER LFKPWAIFTR QDIKIAVIGL TTDDTAKIGN 190 200 210 220 230 240 PEYFTDIEFR KPAEEAKVVI QELNMNEKPD VIIATTHMGH YDNGDHGSNA PGDVEMARSL 250 260 270 280 290 300 PAGSLAMIVG GHSQDPVCMA SENKKQVNYV PGTPCAPDKQ NGIWIVQAHE WGKYVGRADF 310 320 330 340 350 360 EFRNGEMKMV NYQLIPVNLK KKVTWDNGKS ERVLYTPEIA ENPQMLLLLT PFQNKGKVQL 370 380 390 400 410 420 EVKIGSVNGL LEGDRSKVRF VQTNMGRVIL AAQIARTGAD FGVMSGGGIR DSIEAGDITY 430 440 450 460 470 480 KSVLKVQPFG NIVVYADMSG KEVVDYLTRV AQMKPDSGAY PQLANVSFVA KEGKLTDLKI 490 500 510 520 530 540 KGEPVDPAKT YRMATLSFNA TGGDGYPRID NKPGYVNTGF IDAEVLKEFI QQNSPLDAAA 550 FTPKGEVSWL

References

[1]

"The cryptic ushA gene (ushA(c)) in natural isolates of Salmonella enterica (serotype Typhimurium) has been inactivated by a single missense mutation." Innes D., Beacham I.R., Beven C.-A., Douglas M., Laird M.W., Joly J.C., Burns D.M. Microbiology 147:1887-1896(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF188727 Genomic DNA. Translation: AAF05581.1.
3D structure databases
ProteinModelPortal	Q9RN37.
SMR	Q9RN37. Positions 26-549.
ModBase	Search...
Proteomic databases
PRIDE	Q9RN37.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.90.780.10. 1 hit.
InterPro	IPR008334. 5'-Nucleotdase_C. IPR006146. 5'-Nucleotdase_CS. IPR006179. 5_nucleotidase/apyrase. IPR004843. Metallo_PEstase_dom. [Graphical view]
PANTHER	PTHR11575. PTHR11575. 1 hit.
Pfam	PF02872. 5_nucleotid_C. 1 hit. PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR01607. APYRASEFAMLY.
SUPFAM	SSF55816. 5'-Nucleotdase_C. 1 hit.
PROSITE	PS00785. 5_NUCLEOTIDASE_1. 1 hit. PS00786. 5_NUCLEOTIDASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

USHA_SALPU

Accession

Primary (citable) accession number: Q9RN37

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2003
Last sequence update:	May 1, 2000
Last modified:	April 3, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program