ID   TPA_BILW3               Reviewed;         456 AA.
AC   E5Y945;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Taurine--pyruvate aminotransferase {ECO:0000305|PubMed:30718429};
DE            EC=2.6.1.77 {ECO:0000269|PubMed:30718429};
DE   AltName: Full=Taurine:pyruvate aminotransferase {ECO:0000303|PubMed:30718429};
GN   Name=tpa {ECO:0000303|PubMed:30718429};
GN   ORFNames=HMPREF0179_02713 {ECO:0000312|EMBL:EFV43470.1};
OS   Bilophila wadsworthia (strain 3_1_6).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Bilophila.
OX   NCBI_TaxID=563192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_6;
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Sibley C., Strauss J.,
RA   Allen-Vercoe E., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M.,
RA   Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J.,
RA   McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bilophila wadsworthia 3_1_6.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INDUCTION BY TAURINE, AND PATHWAY.
RC   STRAIN=3_1_6;
RX   PubMed=30718429; DOI=10.1073/pnas.1815661116;
RA   Peck S.C., Denger K., Burrichter A., Irwin S.M., Balskus E.P.,
RA   Schleheck D.;
RT   "A glycyl radical enzyme enables hydrogen sulfide production by the human
RT   intestinal bacterium Bilophila wadsworthia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 116:3171-3176(2019).
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.
CC       {ECO:0000269|PubMed:30718429}.
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:30718429};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10421;
CC         Evidence={ECO:0000269|PubMed:30718429};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000305|PubMed:30718429};
CC   -!- PATHWAY: Organosulfur degradation; alkanesulfonate degradation.
CC       {ECO:0000269|PubMed:30718429}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9APM5}.
CC   -!- INDUCTION: Highly up-regulated in the presence of taurine.
CC       {ECO:0000269|PubMed:30718429}.
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|PubMed:30718429}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; ADCP02000001; EFV43470.1; -; Genomic_DNA.
DR   RefSeq; WP_005028753.1; NZ_KE150238.1.
DR   AlphaFoldDB; E5Y945; -.
DR   SMR; E5Y945; -.
DR   STRING; 563192.HMPREF0179_02713; -.
DR   EnsemblBacteria; EFV43470; EFV43470; HMPREF0179_02713.
DR   eggNOG; COG0161; Bacteria.
DR   HOGENOM; CLU_016922_4_0_7; -.
DR   UniPathway; UPA00338; -.
DR   Proteomes; UP000006034; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; Pyridoxal phosphate; Pyruvate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..456
FT                   /note="Taurine--pyruvate aminotransferase"
FT                   /id="PRO_0000450940"
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