Alpha-ketoglutarate-dependent taurine dioxygenase

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P37610 (TAUD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 104. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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. Source: EcoliWiki
Molecular function	L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion binding Inferred from physical interaction Ref.9. Source: EcoliWiki 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 Ref.8. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 283

282

Alpha-ketoglutarate-dependent taurine dioxygenase

PRO_0000194016

Sites

Metal binding

Iron; catalytic

Metal binding

101

Iron; catalytic

Metal binding

255

Iron; catalytic

Binding site

Substrate

Binding site

Substrate

Binding site

Substrate

Binding site

102

Substrate; via amide nitrogen

Binding site

126

2-oxoglutarate

Binding site

240

2-oxoglutarate

Binding site

266

2-oxoglutarate

Binding site

270

2-oxoglutarate

Binding site

270

Substrate

Amino acid modifications

Modified residue

128

3-hydroxytryptophan; by autocatalysis

Modified residue

240

3-hydroxytryptophan; by autocatalysis

Modified residue

248

3-hydroxytryptophan; by autocatalysis

Secondary structure

283

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P37610 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7ADEB0CDC9CEEB57
Show »

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

« Hide

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: 8808933] [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: 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 structure of the Escherichia coli hemB gene." Li J.-M., Russell C.S., Cosloy S.D. Gene 75:177-184(1989) [PubMed: 2656410] [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: 8774726] [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: 7984428] [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: 9287300] [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: 11955067] [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: 12741810] [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.

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.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000002767; EBESCP00000002767; EBESCG00000002257.
EBESCT00000016698; EBESCP00000015989; EBESCG00000015757.

GeneID

945021.

GenomeReviews

Gene locus JW0360 in contig AP009048_GR.
Gene locus b0368 in contig U00096_GR.

KEGG

ecj:JW0360.
eco:b0368.

PATRIC

32115875. VBIEscCol129921_0379.

Organism-specific databases

EchoBASE

EB2322.

EcoGene

EG12423. tauD.

Phylogenomic databases

eggNOG

COG2175.

GeneTree

EBGT00050000008564.

HOGENOM

HBG692281.

OMA

LLFAHAT.

PhylomeDB

P37610.

ProtClustDB

PRK09553.

Enzyme and pathway databases

BioCyc

EcoCyc:MONOMER0-147.
MetaCyc:MONOMER0-147.

Gene expression databases

Genevestigator

P37610.

Family and domain databases

InterPro

IPR003819. Taurine_dOase.
[Graphical view]

K03119.

Pfam

PF02668. TauD. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	January 25, 2012
This is version 104 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents