TPA_BILWA
ID TPA_BILWA Reviewed; 456 AA.
AC Q9APM5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Taurine--pyruvate aminotransferase {ECO:0000305|PubMed:11082195};
DE EC=2.6.1.77 {ECO:0000269|PubMed:11082195};
DE AltName: Full=Taurine:pyruvate aminotransferase {ECO:0000303|PubMed:11082195};
GN Name=tpa {ECO:0000303|PubMed:11082195};
OS Bilophila wadsworthia.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Bilophila.
OX NCBI_TaxID=35833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-28; 101-119 AND
RP 363-372, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, PATHWAY, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=DSM 11045 / RZATAU;
RX PubMed=11082195; DOI=10.1046/j.1432-1033.2000.01782.x;
RA Laue H., Cook A.M.;
RT "Biochemical and molecular characterization of taurine:pyruvate
RT aminotransferase from the anaerobe Bilophila wadsworthia.";
RL Eur. J. Biochem. 267:6841-6848(2000).
CC -!- FUNCTION: Involved in an anaerobic respiration pathway that converts
CC the sulfonate taurine (2-aminoethanesulfonate) to ammonia, acetate and
CC sulfide. Catalyzes the initial metabolic reaction of anaerobic taurine
CC degradation, i.e. the transamination reaction between taurine and
CC pyruvate leading to sulfoacetaldehyde and alanine. Is also able to
CC transaminate hypotaurine (2-aminosulfinate), beta-alanine and with low
CC activity cysteine and 3-aminopropanesulfonate in vitro. In addition to
CC pyruvate, 2-oxobutyrate and oxaloacetate can also be used as amino
CC group acceptors. {ECO:0000269|PubMed:11082195}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyruvate + taurine = L-alanine + sulfoacetaldehyde;
CC Xref=Rhea:RHEA:10420, ChEBI:CHEBI:15361, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:58246, ChEBI:CHEBI:507393; EC=2.6.1.77;
CC Evidence={ECO:0000269|PubMed:11082195};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10421;
CC Evidence={ECO:0000305|PubMed:11082195};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hypotaurine + pyruvate = 2-sulfinoacetaldehyde + L-alanine;
CC Xref=Rhea:RHEA:58056, ChEBI:CHEBI:15361, ChEBI:CHEBI:57853,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:142501; EC=2.6.1.77;
CC Evidence={ECO:0000269|PubMed:11082195};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxopropanoate + L-alanine = beta-alanine + pyruvate;
CC Xref=Rhea:RHEA:14077, ChEBI:CHEBI:15361, ChEBI:CHEBI:33190,
CC ChEBI:CHEBI:57966, ChEBI:CHEBI:57972;
CC Evidence={ECO:0000269|PubMed:11082195};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:11082195};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.1 mM for taurine {ECO:0000269|PubMed:11082195};
CC KM=0.82 mM for pyruvate {ECO:0000269|PubMed:11082195};
CC KM=8.1 mM for hypotaurine {ECO:0000269|PubMed:11082195};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:11082195};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:11082195};
CC -!- PATHWAY: Organosulfur degradation; alkanesulfonate degradation.
CC {ECO:0000269|PubMed:11082195}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11082195}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11082195}.
CC -!- MISCELLANEOUS: Taurine is an abundant dietary and host-derived molecule
CC whose metabolism to hydrogen sulfide (H2S) by members of the human gut
CC microbiota has many prominent connections to host health and disease.
CC The human gut bacterium and opportunistic pathogen Bilophila
CC wadsworthia produces H2S when respiring sulfite (HSO3-) released from
CC organosulfonate substrates such as taurine and isethionate.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AF269146; AAG50296.1; -; Genomic_DNA.
DR RefSeq; WP_005028753.1; NZ_CABKPK010000001.1.
DR AlphaFoldDB; Q9APM5; -.
DR SMR; Q9APM5; -.
DR PRIDE; Q9APM5; -.
DR KEGG; ag:AAG50296; -.
DR BioCyc; MetaCyc:MON-2981; -.
DR BRENDA; 2.6.1.77; 856.
DR SABIO-RK; Q9APM5; -.
DR UniPathway; UPA00338; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016223; F:beta-alanine-pyruvate transaminase activity; IEA:RHEA.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0046306; P:alkanesulfonate catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Cytoplasm; Direct protein sequencing;
KW Pyridoxal phosphate; Pyruvate; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11082195"
FT CHAIN 2..456
FT /note="Taurine--pyruvate aminotransferase"
FT /id="PRO_0000120534"
FT MOD_RES 280
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P42588"
SQ SEQUENCE 456 AA; 49721 MW; 9BCB695DA32C77A9 CRC64;
MTYDKAELVA LDKKYVWHHL TQHKNFEPAI YVKGEGMRIT DIDGKTYLDA VSGGVWTVNV
GYGRKEIVDA VAKQMMEMCY FANGIGNVPT IKFSEKLISK MPGMSRVYLS NSGSEANEKA
FKIVRQIGQL KHGGKKTGIL YRARDYHGTT IGTLSACGQF ERKVQYGPFA PGFYEFPDCD
VYRSKFGDCA DLGVKMAKQL EEVILTVGPD ELGAVIVEPM TAGGGILVPP AGYYETIREI
CDKYELLLII DEVVCGLGRT GKWFGYQHFN VQPDIVTMAK GVASGYAPIS CTVTTEKVFQ
DFVNDPADTD AYFRDISTFG GCTSGPAAAL ANIEIIEREN LLENCTKMGD RLLEGLKGLM
AKHPIIGDVR GKGLFAGIEI VKDRATKEPI AEAVANAMVG AAKQAGVLIG KTSRSFREFN
NTLTLCPALI ATEADIDEIV AGIDKAFTTV EQKFGL
