Reviewed, UniProtKB/Swiss-Prot P07024 (USHA_ECOLI)

Names and origin

Protein names

Recommended name:
    Protein ushA
Including the following 2 domains:
    1- Recommended name:
            UDP-sugar hydrolase
              EC=3.6.1.45
        Alternative name(s):
            UDP-sugar pyrophosphatase
            UDP-sugar diphosphatase
    2- Recommended name:
            5'-nucleotidase
                Short name=5'-NT
              EC=3.1.3.5

Gene names

Name:	ushA
Ordered Locus Names:	b0480, JW0469

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	550 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell.
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.
Enzyme regulation	The activity of this protein is inhibited by an intracellular protein inhibitor.
Subunit structure	Monomer.
Subcellular location	Periplasm. Note: Exported from the cell, except a small proportion that is internally localized.
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
Technical term	3D-structure Complete proteome Direct protein sequencing
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 nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW zinc 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

Signal peptide

1 – 25

25

Ref.1 Ref.6

Chain

26 – 550

525

Protein ushA

PRO_0000000031

Regions

Region

375 – 379

5

Substrate binding

Region

498 – 504

7

Substrate binding

Sites

Metal binding

41

1

Zinc 1

Metal binding

43

1

Zinc 1

Metal binding

84

1

Zinc 1

Metal binding

84

1

Zinc 2

Metal binding

116

1

Zinc 2

Metal binding

217

1

Zinc 2

Metal binding

252

1

Zinc 2

Metal binding

254

1

Zinc 1

Site

117

1

Transition state stabilizer

Site

120

1

Transition state stabilizer

Amino acid modifications

Disulfide bond

258 ↔ 275

Experimental info

Sequence conflict

256

1

P → T in CAA27532. Ref.1

Secondary structure

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550

Helix Strand Turn

Details...

Beta strand

31 – 39

9

Helix

56 – 72

17

Beta strand

76 – 81

6

Beta strand

86 – 89

4

Helix

90 – 93

4

Turn

94 – 97

4

Helix

98 – 107

10

Beta strand

111 – 113

3

Helix

116 – 119

4

Helix

123 – 132

10

Beta strand

140 – 144

5

Turn

145 – 147

3

Beta strand

150 – 160

11

Beta strand

163 – 171

9

Helix

175 – 178

4

Helix

181 – 184

4

Beta strand

187 – 189

3

Helix

192 – 206

15

Beta strand

210 – 218

9

Helix

222 – 224

3

Helix

233 – 239

7

Beta strand

244 – 249

6

Beta strand

259 – 261

3

Beta strand

278 – 280

3

Beta strand

283 – 286

4

Beta strand

293 – 303

11

Beta strand

306 – 318

13

Beta strand

320 – 324

5

Beta strand

330 – 336

7

Helix

343 – 354

12

Helix

357 – 360

4

Beta strand

363 – 369

7

Helix

375 – 378

4

Helix

384 – 397

14

Beta strand

400 – 405

6

Helix

406 – 408

3

Beta strand

415 – 419

5

Helix

420 – 426

7

Beta strand

432 – 439

8

Helix

440 – 451

12

Beta strand

455 – 457

3

Beta strand

461 – 465

5

Beta strand

487 – 496

10

Helix

497 – 500

4

Helix

503 – 505

3

Beta strand

512 – 514

3

Beta strand

516 – 521

6

Helix

522 – 533

12

Helix

538 – 541

4

Beta strand

545 – 547

3

Sequences

	Sequence		Length	Mass (Da)
	P07024-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: DBA07B1C40C6C075	FASTA	550	60,824
	10 20 30 40 50 60 MKLLQRGVAL ALLTTFTLAS ETALAYEQDK TYKITVLHTN DHHGHFWRNE YGEYGLAAQK 70 80 90 100 110 120 TLVDGIRKEV AAEGGSVLLL SGGDINTGVP ESDLQDAEPD FRGMNLVGYD AMAIGNHEFD 130 140 150 160 170 180 NPLTVLRQQE KWAKFPLLSA NIYQKSTGER LFKPWALFKR QDLKIAVIGL TTDDTAKIGN 190 200 210 220 230 240 PEYFTDIEFR KPADEAKLVI QELQQTEKPD IIIAATHMGH YDNGEHGSNA PGDVEMARAL 250 260 270 280 290 300 PAGSLAMIVG GHSQDPVCMA AENKKQVDYV PGTPCKPDQQ NGIWIVQAHE WGKYVGRADF 310 320 330 340 350 360 EFRNGEMKMV NYQLIPVNLK KKVTWEDGKS ERVLYTPEIA ENQQMISLLS PFQNKGKAQL 370 380 390 400 410 420 EVKIGETNGR LEGDRDKVRF VQTNMGRLIL AAQMDRTGAD FAVMSGGGIR DSIEAGDISY 430 440 450 460 470 480 KNVLKVQPFG NVVVYADMTG KEVIDYLTAV AQMKPDSGAY PQFANVSFVA KDGKLNDLKI 490 500 510 520 530 540 KGEPVDPAKT YRMATLNFNA TGGDGYPRLD NKPGYVNTGF IDAEVLKAYI QKSSPLDVSV 550 YEPKGEVSWQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and transcriptional analysis of the E. coli ushA gene, encoding periplasmic UDP-sugar hydrolase (5'-nucleotidase): regulation of the ushA gene, and the signal sequence of its encoded protein product." Burns D.M., Beacham I.R. Nucleic Acids Res. 14:4325-4342(1986) [PubMed: 3012467] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-27.
[2]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"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.
[4]	"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.
[5]	Fujisaki S., Ohnuma S., Horiuchi T., Takahashi I., Tsukui S., Nishimura Y., Nishino T., Inokuchi H. Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41. Strain: K12 / DH5-alpha.
[6]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-37. Strain: K12 / EMG2.
[7]	"X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site." Knoefel T., Straeter N. Nat. Struct. Biol. 6:448-453(1999) [PubMed: 10331872] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 26-550.
[8]	"Mechanism of hydrolysis of phosphate esters by the dimetal center of 5'-nucleotidase based on crystal structures." Knoefel T., Straeter N. J. Mol. Biol. 309:239-254(2001) [PubMed: 11491293] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; PRODUCT AND INHIBITOR.
[9]	"E. coli 5'-nucleotidase undergoes a hinge-bending domain rotation resembling a ball-and-socket motion." Knoefel T., Straeter N. J. Mol. Biol. 309:255-266(2001) [PubMed: 11491294] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X03895 Genomic DNA. Translation: CAA27532.1.
U82664 Genomic DNA. Translation: AAB40234.1.
U00096 Genomic DNA. Translation: AAC73582.1.
AP009048 Genomic DNA. Translation: BAE76259.1.
D73370 Genomic DNA. No translation available.

PIR

YXECUG. G64778.

RefSeq

AP_001129.1.
NP_415013.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HO5	X-ray	2.10	A/B	26-550	[»]
1HP1	X-ray	1.70	A	26-550	[»]
1HPU	X-ray	1.85	A/B/C/D	26-550	[»]
1OI8	X-ray	2.10	A/B	26-550	[»]
1OID	X-ray	2.10	A/B	26-550	[»]
1OIE	X-ray	2.33	A	26-550	[»]
1USH	X-ray	1.73	A	1-550	[»]
2USH	X-ray	2.22	A/B	1-550	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:11096N.

2-D gel databases

2DBase-Ecoli

P07024.

Genome annotation databases

GeneID

947331.

GenomeReviews

Gene locus JW0469 in contig AP009048_GR.
Gene locus b0480 in contig U00096_GR.

KEGG

ecj:JW0469.
eco:b0480.

Organism-specific databases

EchoBASE

EB1053.

EcoGene

EG11060. ushA.

CMR

Search...

Phylogenomic databases

HOGENOM

P07024.

OMA

P07024. EAAHHYG.

Enzyme and pathway databases

BioCyc

EcoCyc:USHA-MON.
MetaCyc:USHA-MON.

Family and domain databases

InterPro

IPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase.
IPR004843. M-pesterase.
[Graphical view]

Gene3D

G3DSA:3.90.780.10. 5'-Nucleotdase_C. 1 hit.

PANTHER

PTHR11575. 5_nucleotidase. 1 hit.

Pfam

PF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]

PRINTS

PR01607. APYRASEFAMLY.

PROSITE

PS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

USHA_ECOLI

Accession

Primary (citable) accession number: P07024
Secondary accession number(s): P78274, Q2MBU7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)