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TPL_ENTAG
ID   TPL_ENTAG               Reviewed;         456 AA.
AC   P31011;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Tyrosine phenol-lyase;
DE            EC=4.1.99.2;
DE   AltName: Full=Beta-tyrosinase;
GN   Name=tpl; Synonyms=tutA;
OS   Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX   NCBI_TaxID=549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MT-10509;
RX   PubMed=1418690;
RA   Iwamori S., Oikawa T., Ishiwata K., Makiguchi N.;
RT   "Cloning and expression of the Erwinia herbicola tyrosine phenol-lyase gene
RT   in Escherichia coli.";
RL   Biotechnol. Appl. Biochem. 16:77-85(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-11.
RC   STRAIN=AJ2982;
RA   Suzuki H., Nishihara K., Usui N., Matsui H., Kumagai H.;
RT   "Cloning and nucleotide sequence of Erwinia herbicola AJ2982 tyrosine
RT   phenol-lyase gene.";
RL   J. Ferment. Bioeng. 75:145-148(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21434 / AJ 2985;
RA   Foor F.;
RL   Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51.
RX   PubMed=8215376; DOI=10.1128/aem.59.9.3070-3075.1993;
RA   Foor F., Morin N., Bostian K.;
RT   "Production of L-dihydroxyphenylalanine in Escherichia coli with the
RT   tyrosine phenol-lyase gene cloned from Erwinia herbicola.";
RL   Appl. Environ. Microbiol. 59:3070-3075(1993).
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   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: By L-tyrosine.
CC   -!- PTM: Contains L-DOPA (3',4'-dihydroxyphenylalanine).
CC   -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC       {ECO:0000305}.
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DR   EMBL; S50513; AAB24234.1; -; Genomic_DNA.
DR   EMBL; D13714; BAA02867.1; -; Genomic_DNA.
DR   EMBL; U25347; AAA66390.1; -; Genomic_DNA.
DR   EMBL; L08484; AAA71928.1; -; Genomic_DNA.
DR   PDB; 1C7G; X-ray; 2.10 A; A/B/C/D=1-456.
DR   PDBsum; 1C7G; -.
DR   AlphaFoldDB; P31011; -.
DR   SMR; P31011; -.
DR   PRIDE; P31011; -.
DR   EvolutionaryTrace; P31011; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   3D-structure; Cytoplasm; Direct protein sequencing; Lyase;
KW   Pyridoxal phosphate.
FT   CHAIN           1..456
FT                   /note="Tyrosine phenol-lyase"
FT                   /id="PRO_0000195633"
FT   MOD_RES         257
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   VARIANT         157
FT                   /note="D -> N (in strain: MT-10509)"
FT   VARIANT         212
FT                   /note="F -> Y (in strain: MT-10509)"
FT   VARIANT         397
FT                   /note="R -> S (in strain: MT-10509)"
FT   VARIANT         420
FT                   /note="V -> I (in strain: MT-10509)"
FT   STRAND          7..15
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           21..30
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   TURN            31..33
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           40..42
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           58..63
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   STRAND          71..73
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           75..88
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   STRAND          91..98
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           99..110
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   STRAND          115..121
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           124..132
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   STRAND          135..139
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           143..146
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           160..170
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           172..174
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   STRAND          175..184
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   TURN            185..188
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           194..207
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   STRAND          211..214
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           218..228
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           237..245
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   STRAND          249..254
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   TURN            255..259
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   STRAND          265..270
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           272..285
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   TURN            289..293
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           296..309
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           312..331
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   STRAND          342..348
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           349..352
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           358..360
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           362..374
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   STRAND          375..377
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   STRAND          379..382
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           383..386
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   STRAND          390..392
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   STRAND          402..406
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           414..428
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           429..433
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   STRAND          437..441
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   STRAND          444..446
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   HELIX           447..450
FT                   /evidence="ECO:0007829|PDB:1C7G"
FT   STRAND          452..455
FT                   /evidence="ECO:0007829|PDB:1C7G"
SQ   SEQUENCE   456 AA;  51365 MW;  34758B48AF7C4AE2 CRC64;
     MNYPAEPFRI KSVETVSMIS RDERVKKMQE AGYNTFLLNS KDIYIDLLTD SGTNAMSDKQ
     WAGMMIGDEA YAGSENFYHL EKTVKELFGF KHIVPTHQGR GAENLLSQLA IKPGQYVAGN
     MYFTTTRFHQ EKNGATFVDI VRDEAHDASL NLPFKGDIDL NKLATLIKEK GAENIAYICL
     AVTVNLAGGQ PVSMANMRAV HEMASTYGIK IFYDATRCVE NAYFIKEQEA GYENVSIKDI
     VHEMFSYADG CTMSGKKDCL VNIGGFLCMN DEEMFSAAKE LVVVYEGMPS YGGLAGRDME
     AMAIGLREAM QYEYIEHRVK QVRYLGDKLR EAGVPIVEPT GGHAVFLDAR RFCPHLTQDQ
     FPAQSLAASI YMETGVRSME RGIVSAGRSK ETGENHRPKL ETVRLTIPRR VYTYAHMDVV
     ADGIIKLYQH KEDIRGLTFV YEPKQLRFFT ARFDFI
 
 
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