ID   TPL_SYMTH               Reviewed;         458 AA.
AC   Q08897; Q67KH1;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Tyrosine phenol-lyase;
DE            EC=4.1.99.2;
DE   AltName: Full=Beta-tyrosinase;
GN   Name=tpl; OrderedLocusNames=STH2842;
OS   Symbiobacterium thermophilum (strain T / IAM 14863).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=292459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-7; 270-279 AND
RP   440-450.
RC   STRAIN=IAM 13621;
RX   PubMed=7763716; DOI=10.1007/bf00192089;
RA   Hirahara T., Horinouchi S., Beppu T.;
RT   "Cloning, nucleotide sequence, and overexpression in Escherichia coli of
RT   the beta-tyrosinase gene from an obligately symbiotic thermophile,
RT   Symbiobacterium thermophilum.";
RL   Appl. Microbiol. Biotechnol. 39:341-346(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T / IAM 14863;
RX   PubMed=15383646; DOI=10.1093/nar/gkh830;
RA   Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA   Ikeda H., Hattori M., Beppu T.;
RT   "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT   that depends on microbial commensalism.";
RL   Nucleic Acids Res. 32:4937-4944(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-tyrosine = NH4(+) + phenol + pyruvate;
CC         Xref=Rhea:RHEA:21704, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15882, ChEBI:CHEBI:28938, ChEBI:CHEBI:58315; EC=4.1.99.2;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable.;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD41827.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D13002; BAA02365.1; -; Genomic_DNA.
DR   EMBL; AP006840; BAD41827.1; ALT_INIT; Genomic_DNA.
DR   PIR; A48380; A48380.
DR   RefSeq; WP_043714225.1; NC_006177.1.
DR   AlphaFoldDB; Q08897; -.
DR   SMR; Q08897; -.
DR   STRING; 292459.STH2842; -.
DR   EnsemblBacteria; BAD41827; BAD41827; STH2842.
DR   KEGG; sth:STH2842; -.
DR   eggNOG; COG3033; Bacteria.
DR   HOGENOM; CLU_047223_0_0_9; -.
DR   OMA; VYTYAHM; -.
DR   OrthoDB; 91973at2; -.
DR   Proteomes; UP000000417; Chromosome.
DR   GO; GO:0050371; F:tyrosine phenol-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006570; P:tyrosine metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00543; Tyr_phenol_lyase; 1.
DR   InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR011166; Beta-eliminating_lyase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR018176; Tryptophanase_CS.
DR   InterPro; IPR013441; Tyr_phenol_ly.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF001386; Trpase; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR02618; tyr_phenol_ly; 1.
DR   PROSITE; PS00853; BETA_ELIM_LYASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..458
FT                   /note="Tyrosine phenol-lyase"
FT                   /id="PRO_0000195638"
FT   MOD_RES         258
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        173
FT                   /note="A -> R (in Ref. 1; BAA02365)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        374
FT                   /note="D -> H (in Ref. 1; BAA02365)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   458 AA;  52163 MW;  77FD1321CCF089B2 CRC64;
     MQRPWAEPYK IKAVEPIRMT TREYREQAIR EAGYNTFLLR SEDVYIDLLT DSGTNAMSDR
     QWGALMMGDE AYAGARSFFR LEEAVREIYG FKYVVPTHQG RGAEHLISRI LIKPGDYIPG
     NMYFTTTRTH QELQGGTFVD VIIDEAHDPQ ASHPFKGNVD IAKFEALIDR VGADKIPYIN
     VALTVNMAGG QPVSMANLRE VRKVCDRHGI RMWSDATRAV ENAYFIKERE EGYQDKPVRE
     ILKEMMSYFD GCTMSGKKDC LVNIGGFLAM NEEWILQKAR EQVVIFEGMP TYGGLAGRDM
     EAIAQGIYEM VDDDYIAHRI HQVRYLGEQL LEAGIPIVQP IGGHAVFLDA RAFLPHIPQD
     QFPAQALAAA LYVDSGVRAM ERGIVSAGRN PQTGEHNYPK LELVRLTIPR RVYTDRHMDV
     VAYSVKHLWK ERDTIRGLRM VYEPPTLRFF TARFEPIS