P37610 (TAUD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-ketoglutarate-dependent taurine dioxygenase
EC=1.14.11.17

Alternative name(s):
2-aminoethanesulfonate dioxygenase
Sulfate starvation-induced protein 3
Short name=SSI3

Gene names

Name:	tauD
Synonyms:	ssiD, yaiG
Ordered Locus Names:	b0368, JW0360

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	283 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	Catalyzes the conversion of taurine and alpha ketoglutarate to sulfite, aminoacetaldehyde and succinate. Required for the utilization of taurine (2-aminoethanesulfonic acid) as an alternative sulfur source. Pentane-sulfonic acid, 3-(N-morpholino)propanesulfonic acid and 1,3-dioxo-2-isoindolineethanesulfonic acid are also substrates for this enzyme.
Catalytic activity	Taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2. Ref.9 Ref.10
Cofactor	Binds 1 Fe2+ ion per subunit. Ref.9 Ref.10
Enzyme regulation	Activated by ascorbate and inhibited by divalent metal ions such as zinc, copper and cobalt.
Pathway	Organosulfur degradation; taurine degradation via aerobic pathway; aminoacetaldehyde and sulfite from taurine: step 1/1.
Subunit structure	Homodimer. Ref.9 Ref.10
Induction	Repressed by sulfate or cysteine.
Sequence similarities	Belongs to the TfdA dioxygenase family.
Biophysicochemical properties	pH dependence: Optimum pH is 6.9.
Sequence caution	The sequence M24488 differs from that shown. Reason: Frameshift at position 244.

Ontologies

Keywords
Ligand	Iron Metal-binding Vitamin C
Molecular function	Dioxygenase Oxidoreductase
PTM	Hydroxylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	sulfur compound metabolic process Inferred from mutant phenotype Ref.1. Source: EcoliWiki
Cellular_component	cytoplasm Inferred from direct assay PubMed 16165092. Source: EcoliWiki
Molecular_function	L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW taurine dioxygenase activity Inferred from direct assay PubMed 16165092Ref.8. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 283

282

Alpha-ketoglutarate-dependent taurine dioxygenase

PRO_0000194016

Sites

Metal binding

99

1

Iron; catalytic

Metal binding

101

1

Iron; catalytic

Metal binding

255

1

Iron; catalytic

Binding site

70

1

Substrate

Binding site

73

1

Substrate

Binding site

95

1

Substrate

Binding site

102

1

Substrate; via amide nitrogen

Binding site

126

1

2-oxoglutarate

Binding site

240

1

2-oxoglutarate

Binding site

266

1

2-oxoglutarate

Binding site

270

1

2-oxoglutarate

Binding site

270

1

Substrate

Amino acid modifications

Modified residue

128

1

3-hydroxytryptophan; by autocatalysis

Modified residue

240

1

3-hydroxytryptophan; by autocatalysis

Modified residue

248

1

3-hydroxytryptophan; by autocatalysis

Secondary structure

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283

Helix Strand Turn

Details...

Beta strand

6 – 14

9

Beta strand

16 – 20

5

Beta strand

23 – 25

3

Helix

29 – 42

14

Beta strand

43 – 47

5

Helix

54 – 62

9

Beta strand

71 – 73

3

Beta strand

79 – 88

10

Turn

101 – 104

4

Beta strand

105 – 107

3

Beta strand

109 – 118

10

Beta strand

126 – 130

5

Helix

131 – 136

6

Helix

140 – 146

7

Beta strand

150 – 153

4

Helix

155 – 158

4

Helix

161 – 163

3

Helix

168 – 180

13

Beta strand

184 – 191

8

Turn

193 – 195

3

Beta strand

198 – 200

3

Turn

204 – 206

3

Beta strand

207 – 213

7

Helix

215 – 228

14

Helix

232 – 234

3

Beta strand

235 – 238

4

Beta strand

245 – 249

5

Beta strand

252 – 257

6

Beta strand

266 – 274

9

Sequences

	Sequence		Length	Mass (Da)
	P37610 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 7ADEB0CDC9CEEB57	FASTA	283	32,410
	10 20 30 40 50 60 MSERLSITPL GPYIGAQISG ADLTRPLSDN QFEQLYHAVL RHQVVFLRDQ AITPQQQRAL 70 80 90 100 110 120 AQRFGELHIH PVYPHAEGVD EIIVLDTHND NPPDNDNWHT DVTFIETPPA GAILAAKELP 130 140 150 160 170 180 STGGDTLWTS GIAAYEALSV PFRQLLSGLR AEHDFRKSFP EYKYRKTEEE HQRWREAVAK 190 200 210 220 230 240 NPPLLHPVVR THPVSGKQAL FVNEGFTTRI VDVSEKESEA LLSFLFAHIT KPEFQVRWRW 250 260 270 280 QPNDIAIWDN RVTQHYANAD YLPQRRIMHR ATILGDKPFY RAG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source." van der Ploeg J.R., Weiss M.A., Saller E., Nashimoto H., Saito N., Kertesz M.A., Leisinger T. J. Bacteriol. 178:5438-5446(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The structure of the Escherichia coli hemB gene." Li J.-M., Russell C.S., Cosloy S.D. Gene 75:177-184(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 237-283. Strain: K12.
[6]	"Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis. Application to the sulfate-starvation response of Escherichia coli." Quadroni M., Staudenmann W., Kertesz M.A., James P. Eur. J. Biochem. 239:773-781(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11; 42-46 AND 59-63, MASS SPECTROMETRY. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[7]	"Intrinsic and extrinsic approaches for detecting genes in a bacterial genome." Borodovsky M., Rudd K.E., Koonin E.V. Nucleic Acids Res. 22:4756-4767(1994) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[8]	"Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli." Eichhorn E., van der Ploeg J.R., Kertesz M.A., Leisinger T. J. Biol. Chem. 272:23031-23036(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[9]	"X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates." Elkins J.M., Ryle M.J., Clifton I.J., Dunning Hotopp J.C., Lloyd J.S., Burzlaff N.I., Baldwin J.E., Hausinger R.P., Roach P.L. Biochemistry 41:5185-5192(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH IRON; 2-OXOGLUTARATE AND TAURINE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.
[10]	"Substrate-induced conformational changes in Escherichia coli taurine/alpha-ketoglutarate dioxygenase and insight into the oligomeric structure." O'Brien J.R., Schuller D.J., Yang V.S., Dillard B.D., Lanzilotta W.N. Biochemistry 42:5547-5554(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH IRON; 2-OXOGLUTARATE AND TAURINE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D85613 Genomic DNA. Translation: BAA12841.1.
U73857 Genomic DNA. Translation: AAB18091.1.
U00096 Genomic DNA. Translation: AAC73471.1.
AP009048 Genomic DNA. Translation: BAE76149.1.
M24488 Genomic DNA. No translation available.

PIR

H64764. S78607.

RefSeq

NP_414902.1. NC_000913.2.
YP_488661.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GQW	X-ray	3.00	A/B	1-283	[»]
1GY9	X-ray	2.50	A/B	1-283	[»]
1OS7	X-ray	2.50	A/B/C/D	1-283	[»]
1OTJ	X-ray	1.90	A/B/C/D	1-283	[»]

ProteinModelPortal

P37610.

SMR

P37610. Positions 2-282.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10966N.

IntAct

P37610. 4 interactions.

STRING

511145.b0368.

Proteomic databases

PRIDE

P37610.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73471; AAC73471; b0368.
BAE76149; BAE76149; BAE76149.

GeneID

12930836.
945021.

KEGG

ecj:Y75_p0357.
eco:b0368.

PATRIC

32115875. VBIEscCol129921_0379.

Organism-specific databases

EchoBASE

EB2322.

EcoGene

EG12423. tauD.

Phylogenomic databases

eggNOG

COG2175.

HOGENOM

HOG000165071.

KO

K03119.

OMA

LLFAHAT.

ProtClustDB

PRK09553.

Enzyme and pathway databases

BioCyc

EcoCyc:MONOMER0-147.
ECOL316407:JW0360-MONOMER.
MetaCyc:MONOMER0-147.

SABIO-RK

P37610.

UniPathway

UPA00336; UER00542.

Gene expression databases

Genevestigator

P37610.

Family and domain databases

InterPro

IPR003819. Taurine_dOase.
[Graphical view]

Pfam

PF02668. TauD. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P37610.

Entry information

Entry name

TAUD_ECOLI

Accession

Primary (citable) accession number: P37610
Secondary accession number(s): P77797, Q2MC57, Q47540

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program