Reviewed, UniProtKB/Swiss-Prot P07649 (TRUA_ECOLI)

Names and origin

Protein names

Recommended name:
    tRNA pseudouridine synthase A
    EC=5.4.99.12
Alternative name(s):
    tRNA-uridine isomerase I
    tRNA pseudouridylate synthase I
      Short name=PSU-I

Gene names

Name:	truA
Synonyms:	asuC, hisT, leuK
Ordered Locus Names:	b2318, JW2315

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. HAMAP MF_00171
Catalytic activity	tRNA uridine = tRNA pseudouridine. HAMAP MF_00171
Subunit structure	Homodimer. Ref.10
Sequence similarities	Belongs to the tRNA pseudouridine synthase truA family.

Ontologies

Keywords
Biological process	tRNA processing
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	tRNA pseudouridine synthesis Inferred from electronic annotation. Source: HAMAP
Molecular function	pseudouridine synthase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 270

270

tRNA pseudouridine synthase A HAMAP MF_00171

PRO_0000057375

Regions

Region

107 – 111

5

RNA binding Probable

Sites

Active site

60

1

Nucleophile Ref.8 Ref.9

Binding site

118

1

Substrate By similarity

Binding site

245

1

Substrate By similarity

Secondary structure

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270

Helix Strand Turn

Details...

Beta strand

10 – 18

9

Helix

35 – 47

13

Beta strand

53 – 57

5

Beta strand

64 – 75

12

Helix

80 – 89

10

Beta strand

95 – 102

8

Turn

109 – 112

4

Beta strand

115 – 123

9

Beta strand

125 – 127

3

Turn

131 – 134

4

Beta strand

135 – 138

4

Helix

145 – 152

8

Helix

153 – 155

3

Beta strand

157 – 160

4

Helix

162 – 164

3

Beta strand

175 – 186

12

Beta strand

189 – 197

9

Helix

203 – 215

13

Helix

223 – 230

8

Helix

233 – 235

3

Beta strand

245 – 251

7

Helix

254 – 256

3

Sequences

	Sequence		Length	Mass (Da)
	P07649-1 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 8E97BC88C3220188	FASTA	270	30,400
	10 20 30 40 50 60 MSDQQQPPVY KIALGIEYDG SKYYGWQRQN EVRSVQEKLE KALSQVANEP ITVFCAGRTD 70 80 90 100 110 120 AGVHGTGQVV HFETTALRKD AAWTLGVNAN LPGDIAVRWV KTVPDDFHAR FSATARRYRY 130 140 150 160 170 180 IIYNHRLRPA VLSKGVTHFY EPLDAERMHR AAQCLLGEND FTSFRAVQCQ SRTPWRNVMH 190 200 210 220 230 240 INVTRHGPYV VVDIKANAFV HHMVRNIVGS LMEVGAHNQP ESWIAELLAA KDRTLAAATA 250 260 270 KAEGLYLVAV DYPDRYDLPK PPMGPLFLAD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural features of the hisT operon of Escherichia coli K-12." Arps P.J., Marvel C.C., Rubin B.C., Tolan D.A., Penhoet E.E., Winkler M.E. Nucleic Acids Res. 13:5297-5315(1985) [PubMed: 2991861] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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]	"The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons." Nonet M.L., Marvel C.C., Tolan D.R. J. Biol. Chem. 262:12209-12217(1987) [PubMed: 3040734] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 255-270. Strain: K12.
[6]	"Structural analysis of the Escherichia coli K-12 hisT operon by using a kanamycin resistance cassette." Arps P.J., Winkler M.E. J. Bacteriol. 169:1061-1070(1987) [PubMed: 3029016] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10 AND 267-270. Strain: K12.
[7]	"Purification, structure, and properties of Escherichia coli tRNA pseudouridine synthase I." Kammen H.O., Marvel C.C., Hardy L., Penhoet E.E. J. Biol. Chem. 263:2255-2263(1988) [PubMed: 3276686] [Abstract] Cited for: PROTEIN SEQUENCE, CHARACTERIZATION.
[8]	"A conserved aspartate of tRNA pseudouridine synthase is essential for activity and a probable nucleophilic catalyst." Huang L., Pookanjanatavip M., Gu X., Santi D.V. Biochemistry 37:344-351(1998) [PubMed: 9425056] [Abstract] Cited for: ACTIVE SITE.
[9]	"The mechanism of pseudouridine synthase I as deduced from its interaction with 5-fluorouracil-tRNA." Gu X., Liu Y., Santi D.V. Proc. Natl. Acad. Sci. U.S.A. 96:14270-14275(1999) [PubMed: 10588695] [Abstract] Cited for: ACTIVE SITE.
[10]	"The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I." Foster P.G., Huang L., Santi D.V., Stroud R.M. Nat. Struct. Biol. 7:23-27(2000) [PubMed: 10625422] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X02743 Genomic DNA. Translation: CAA26522.1.
U00096 Genomic DNA. Translation: AAC75378.1.
AP009048 Genomic DNA. Translation: BAA16175.1.
M68934 Genomic DNA. Translation: AAA23963.1.
M15542 Genomic DNA. Translation: AAA24313.1.
M15543 Genomic DNA. No translation available.

PIR

SYECZ1. B23792.

RefSeq

AP_002918.1.
NP_416821.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DJ0	X-ray	1.50	A/B	7-270	[»]
2NQP	X-ray	3.50	A/B/C/D	7-270	[»]
2NR0	X-ray	3.90	A/B/C/D	7-270	[»]
2NRE	X-ray	4.00	A	7-270	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:11043N.

Genome annotation databases

GeneID

946793.

GenomeReviews

Gene locus JW2315 in contig AP009048_GR.
Gene locus b2318 in contig U00096_GR.

KEGG

ecj:JW2315.
eco:b2318.

Organism-specific databases

EchoBASE

EB0449.

EcoGene

EG10454. truA.

CMR

Search...

Phylogenomic databases

HOGENOM

P07649.

OMA

P07649. RRYRYTI.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10454-MON.
MetaCyc:EG10454-MON.

BRENDA

5.4.99.12. 246.

Family and domain databases

HAMAP

MF_00171.
[Tree]

InterPro

IPR001406. tRNA_psdUrid_synth.
[Graphical view]

Gene3D

G3DSA:3.30.70.580. PseudoU_synth_1. 1 hit.
G3DSA:3.30.70.660. PseudoU_synth_1. 1 hit.

PANTHER

PTHR11142. PseudoU_synth_1. 1 hit.

Pfam

PF01416. PseudoU_synth_1. 2 hits.
[Graphical view]

PIRSF

PIRSF001430. tRNA_psdUrid_synth. 1 hit.

TIGRFAMs

TIGR00071. hisT_truA. 1 hit.

ProtoNet

Search...

Entry information

Entry name

TRUA_ECOLI

Accession

Primary (citable) accession number: P07649

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	June 16, 2009
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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