TAUD_PSEPK
ID TAUD_PSEPK Reviewed; 277 AA.
AC Q88RA3;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Alpha-ketoglutarate-dependent taurine dioxygenase {ECO:0000303|PubMed:22221834};
DE EC=1.14.11.17 {ECO:0000269|PubMed:22221834};
GN Name=tauD {ECO:0000303|PubMed:22221834};
GN Synonyms=atsK {ECO:0000312|EMBL:AAN65862.1};
GN OrderedLocusNames=PP_0230 {ECO:0000312|EMBL:AAN65862.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [2] {ECO:0007744|PDB:3PVJ, ECO:0007744|PDB:3V15, ECO:0007744|PDB:3V17}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP 2-OXOGLUTARATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=22221834; DOI=10.1111/j.1742-4658.2012.08473.x;
RA Knauer S.H., Hartl-Spiegelhauer O., Schwarzinger S., Hanzelmann P.,
RA Dobbek H.;
RT "The Fe(II)/alpha-ketoglutarate-dependent taurine dioxygenases from
RT Pseudomonas putida and Escherichia coli are tetramers.";
RL FEBS J. 279:816-831(2012).
CC -!- FUNCTION: Catalyzes the alpha-ketoglutarate-dependent hydroxylation of
CC taurine yielding sulfite and aminoacetaldehyde after decomposition of
CC an unstable intermediate. {ECO:0000269|PubMed:22221834}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + O2 + taurine = aminoacetaldehyde + CO2 + H(+)
CC + succinate + sulfite; Xref=Rhea:RHEA:15909, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:30031, ChEBI:CHEBI:58213,
CC ChEBI:CHEBI:507393; EC=1.14.11.17;
CC Evidence={ECO:0000269|PubMed:22221834};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:22221834};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:22221834};
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000269|PubMed:22221834}.
CC -!- INTERACTION:
CC Q88RA3; Q88RA3: tauD; NbExp=2; IntAct=EBI-7634056, EBI-7634056;
CC -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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DR EMBL; AE015451; AAN65862.1; -; Genomic_DNA.
DR RefSeq; NP_742398.1; NC_002947.4.
DR RefSeq; WP_010951611.1; NC_002947.4.
DR PDB; 3PVJ; X-ray; 1.85 A; A/B/C/D=1-277.
DR PDB; 3V15; X-ray; 2.60 A; A/B/C/D=1-277.
DR PDB; 3V17; X-ray; 2.57 A; A/B/C/D=1-277.
DR PDBsum; 3PVJ; -.
DR PDBsum; 3V15; -.
DR PDBsum; 3V17; -.
DR AlphaFoldDB; Q88RA3; -.
DR SMR; Q88RA3; -.
DR MINT; Q88RA3; -.
DR STRING; 160488.PP_0230; -.
DR EnsemblBacteria; AAN65862; AAN65862; PP_0230.
DR KEGG; ppu:PP_0230; -.
DR PATRIC; fig|160488.4.peg.246; -.
DR eggNOG; COG2175; Bacteria.
DR HOGENOM; CLU_036005_2_1_6; -.
DR OMA; FVDAYPK; -.
DR PhylomeDB; Q88RA3; -.
DR BioCyc; PPUT160488:G1G01-252-MON; -.
DR BRENDA; 1.14.11.17; 5092.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0000907; F:sulfonate dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0000908; F:taurine dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0044273; P:sulfur compound catabolic process; IDA:UniProtKB.
DR Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR Pfam; PF02668; TauD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..277
FT /note="Alpha-ketoglutarate-dependent taurine dioxygenase"
FT /id="PRO_0000448494"
FT BINDING 68
FT /ligand="taurine"
FT /ligand_id="ChEBI:CHEBI:507393"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 71
FT /ligand="taurine"
FT /ligand_id="ChEBI:CHEBI:507393"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 93
FT /ligand="taurine"
FT /ligand_id="ChEBI:CHEBI:507393"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 97
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 99
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 100
FT /ligand="taurine"
FT /ligand_id="ChEBI:CHEBI:507393"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 124
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0007744|PDB:3V17"
FT BINDING 253
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0007744|PDB:3V17"
FT BINDING 253
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 264
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0007744|PDB:3V17"
FT BINDING 268
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0007744|PDB:3V17"
FT BINDING 268
FT /ligand="taurine"
FT /ligand_id="ChEBI:CHEBI:507393"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:3PVJ"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:3PVJ"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:3PVJ"
FT HELIX 27..40
FT /evidence="ECO:0007829|PDB:3PVJ"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:3PVJ"
FT HELIX 52..59
FT /evidence="ECO:0007829|PDB:3PVJ"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:3PVJ"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:3PVJ"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:3PVJ"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:3PVJ"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3PVJ"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:3PVJ"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:3PVJ"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:3PVJ"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:3PVJ"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:3PVJ"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:3PVJ"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:3PVJ"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:3PVJ"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:3PVJ"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:3PVJ"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:3PVJ"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:3PVJ"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:3PVJ"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:3PVJ"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:3PVJ"
FT HELIX 213..227
FT /evidence="ECO:0007829|PDB:3PVJ"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:3PVJ"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:3PVJ"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:3PVJ"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:3PVJ"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:3PVJ"
SQ SEQUENCE 277 AA; 31098 MW; CFA7BB8DDA2DC601 CRC64;
MSLTITPLSP ALGAQISGVD ISRDISAEER DAIEQALLQH QVLFLRDQPI NPEQQARFAA
RFGDLHIHPI YPNVPDTPQV LVLDTAVTDV RDNAVWHTDV TFLPTPALGA VLSAKQLPAY
GGDTLWASGI AAFEALSAPL REMLDGLTAT HDFTKSFPLE RFGTTPQDLA RWEATRRNNP
PLSHPVVRTH PVSGRKALFV NEGFTTRINE LSELESDALL RLLFAHATRP EFSIRWRWQE
NDVAFWDNRV TQHFAVDDYR PNRRVMHRAT ILGDAPF
