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Database: UniProt
Entry: A5EVV3_DICNV
LinkDB: A5EVV3_DICNV
Original site: A5EVV3_DICNV 
ID   A5EVV3_DICNV            Unreviewed;       465 AA.
AC   A5EVV3;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Tyrosine phenol-lyase {ECO:0000256|ARBA:ARBA00016166, ECO:0000256|HAMAP-Rule:MF_00543};
DE            EC=4.1.99.2 {ECO:0000256|ARBA:ARBA00013154, ECO:0000256|HAMAP-Rule:MF_00543};
DE   AltName: Full=Beta-tyrosinase {ECO:0000256|ARBA:ARBA00033449, ECO:0000256|HAMAP-Rule:MF_00543};
GN   Name=tpl {ECO:0000256|HAMAP-Rule:MF_00543};
GN   OrderedLocusNames=DNO_0442 {ECO:0000313|EMBL:ABQ14298.1};
OS   Dichelobacter nodosus (strain VCS1703A).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC   Cardiobacteriaceae; Dichelobacter.
OX   NCBI_TaxID=246195 {ECO:0000313|EMBL:ABQ14298.1, ECO:0000313|Proteomes:UP000000248};
RN   [1] {ECO:0000313|EMBL:ABQ14298.1, ECO:0000313|Proteomes:UP000000248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VCS1703A {ECO:0000313|EMBL:ABQ14298.1,
RC   ECO:0000313|Proteomes:UP000000248};
RX   PubMed=17468768; DOI=10.1038/nbt1302;
RA   Myers G.S., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q.,
RA   Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D.,
RA   McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T.,
RA   Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B.,
RA   Songer J.G., Rood J.I., Paulsen I.T.;
RT   "Genome sequence and identification of candidate vaccine antigens from the
RT   animal pathogen Dichelobacter nodosus.";
RL   Nat. Biotechnol. 25:569-575(2007).
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:0000256|ARBA:ARBA00001821, ECO:0000256|HAMAP-
CC         Rule:MF_00543};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_00543, ECO:0000256|PIRSR:PIRSR611166-50};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC       ECO:0000256|HAMAP-Rule:MF_00543}.
CC   -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC       {ECO:0000256|ARBA:ARBA00009721, ECO:0000256|HAMAP-Rule:MF_00543}.
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DR   EMBL; CP000513; ABQ14298.1; -; Genomic_DNA.
DR   RefSeq; WP_012030780.1; NC_009446.1.
DR   AlphaFoldDB; A5EVV3; -.
DR   STRING; 246195.DNO_0442; -.
DR   KEGG; dno:DNO_0442; -.
DR   eggNOG; COG3033; Bacteria.
DR   HOGENOM; CLU_047223_0_0_6; -.
DR   OrthoDB; 9764079at2; -.
DR   Proteomes; UP000000248; Chromosome.
DR   GO; GO:0050371; F:tyrosine phenol-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006570; P:tyrosine metabolic process; IEA:InterPro.
DR   CDD; cd00617; Tnase_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   NCBIfam; TIGR02618; tyr_phenol_ly; 1.
DR   PANTHER; PTHR32325; BETA-ELIMINATING LYASE-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32325:SF4; TRYPTOPHANASE; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF001386; Trpase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00543, ECO:0000313|EMBL:ABQ14298.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00543}; Reference proteome {ECO:0000313|Proteomes:UP000000248}.
FT   DOMAIN          54..430
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         265
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00543,
FT                   ECO:0000256|PIRSR:PIRSR611166-50"
SQ   SEQUENCE   465 AA;  52460 MW;  85850D5C5D35ABE8 CRC64;
     MSFNFDDLEA YPAEPFKIKS VEPVKMISRA EREKAAKEAG YNTFNLKSED VYIDLLTDSG
     TNAMSDKQWA GMMIGDEAYA GSKNWIYLES VVKDIFGFKH LVPTHQGRGA ENILSRVAIK
     KGQYVPGNMY FTTTRYHQES NGGIFIDIIR DEAHDAQKDV KFKGNVDIDK LKKVIDEHGA
     ENIAYVCLAV TVNLAGGQPV SMQNMREVKE LCSKHGIKVF FDATRFAENA YFIKEQEEGY
     QNKSIKEIVR EMFSYSDGAT CSGKKDGIVN IGGFLALNDD ELFGKAKEIV VVFEGMPSYG
     GMAGRDMQAI AIGLQESLQD EYIEYRIKQV RYLGDKLRQA GVPIVQPTGG HAVFLDAREF
     CPHIPQEQFP AQALAAFLYI DSGVRSMERG IVSAGRDIKT GKNHTPKLET VRLTIPRRVY
     TYRHMDIVAD SVINLYKNNK EIRPLKFTYE PPQLRFFTAR FDFAD
//
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