ID   TPL_LACSW               Reviewed;         468 AA.
AC   D9R201;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Tyrosine phenol-lyase {ECO:0000255|HAMAP-Rule:MF_00543};
DE            EC=4.1.99.2 {ECO:0000255|HAMAP-Rule:MF_00543};
DE   AltName: Full=Beta-tyrosinase {ECO:0000255|HAMAP-Rule:MF_00543};
GN   Name=tpl {ECO:0000255|HAMAP-Rule:MF_00543}; OrderedLocusNames=Closa_0252;
OS   Lacrimispora saccharolytica (strain ATCC 35040 / DSM 2544 / NRCC 2533 /
OS   WM1) (Clostridium saccharolyticum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lacrimispora.
OX   NCBI_TaxID=610130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35040 / DSM 2544 / NRCC 2533 / WM1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Mouttaki H., Lin L., Zhou J., Hemme C.L., Woyke T.;
RT   "Complete sequence of Clostridium saccharolyticum WM1.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00543};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00543};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00543}.
CC   -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00543}.
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DR   EMBL; CP002109; ADL02892.1; -; Genomic_DNA.
DR   RefSeq; WP_013270992.1; NC_014376.1.
DR   AlphaFoldDB; D9R201; -.
DR   SMR; D9R201; -.
DR   STRING; 610130.Closa_0252; -.
DR   PRIDE; D9R201; -.
DR   EnsemblBacteria; ADL02892; ADL02892; Closa_0252.
DR   KEGG; csh:Closa_0252; -.
DR   eggNOG; COG3033; Bacteria.
DR   HOGENOM; CLU_047223_0_0_9; -.
DR   OMA; VYTYAHM; -.
DR   OrthoDB; 91973at2; -.
DR   Proteomes; UP000001662; 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; 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.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..468
FT                   /note="Tyrosine phenol-lyase"
FT                   /id="PRO_0000408492"
FT   MOD_RES         260
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00543"
SQ   SEQUENCE   468 AA;  52639 MW;  B0A9FDF75322A8B6 CRC64;
     MDMMKFAPEP FKIKMVEPMG NLNKEERKDA IRTAGYNTFL LKSEECFIDL LTDSGTNAMS
     DRQWAGLMLG DEAYGGSRNF YHLEETVREL FGFKYVVPTH QGRGAENILS SLTIKPGDYV
     PGNMYFTTTR FHQEHNGATF RDVVIDEAHD PNAILDFKGN IDLNKFQALI DEVGAERIPY
     ICLAVTVNLA GGQPVSMANV KAVSELAHKH GIKVMFDATR CVENAYFIKT REKGYEDKSI
     KEIVHELFSY GDGCTMSGKK DCLTNIGGFL CMNDKDLYIR ATGMVVQYEG MPTYGGMAGR
     DMEAMAIGLR ESMEYNYISH RVNQIRYLGE KLDAAGVPMV KPSGGHAIFV DARAFLDHLD
     QKTDFPAQAL AAAVYEFSGV RTMERGIISA GRDIKTGEDH VPKLETIRLT IPRRVYTYAH
     LDYVADAIIQ LYQMRRDISG LKWVYEPAVL RFFTGRFEPK NGELIKGF