ID TPL_CITFR Reviewed; 456 AA. AC P31013; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 24-JAN-2024, entry version 136. DE RecName: Full=Tyrosine phenol-lyase; DE EC=4.1.99.2; DE AltName: Full=Beta-tyrosinase; GN Name=tpl; OS Citrobacter freundii. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex. OX NCBI_TaxID=546; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 8090 / DSM 30039 / JCM 1657 / LMG 3246 / NCTC 9750; RA Iwamori S., Yoshino S., Ishiwata K., Makiguchi N.; RT "Structure of tyrosine phenol-lyase genes from Citrobacter freundii and RT structural comparison with tryptophanase from Escherichia coli."; RL J. Ferment. Bioeng. 72:147-151(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 254-269; 275-299 AND RP 303-310, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND PYRIDOXAL PHOSPHATE AT RP LYS-257. RX PubMed=7916622; DOI=10.1021/bi00067a006; RA Antson A.A., Demidkina T.V., Gollnick P., Dauter Z., Vontersch R., Long J., RA Berezhnoy S.N., Phillips R.S., Harutyunyan D., Wilson K.S.; RT "Three-dimensional structure of tyrosine phenol-lyase."; RL Biochemistry 32:4195-4206(1993). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). RX PubMed=1601133; DOI=10.1016/0014-5793(92)80454-o; RA Antson A.A., Strokopytov B.V., Murshudov G.N., Isupov M.N., RA Harutyunyan E.H., Demidkina T.V., Vassylyev D.G., Dauter Z., Terry H., RA Wilson K.S.; RT "The polypeptide chain fold in tyrosine phenol-lyase, a pyridoxal-5'- RT phosphate-dependent enzyme."; RL FEBS Lett. 302:256-260(1992). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=9174368; DOI=10.1021/bi962917+; RA Sundararaju B., Antson A.A., Phillips R.S., Demidkina T.V., Barbolina M.V., RA Gollnick P., Dodson G.G., Wilson K.S.; RT "The crystal structure of Citrobacter freundii tyrosine phenol-lyase RT complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site- RT directed mutagenesis and kinetic analysis, demonstrates that arginine 381 RT is required for substrate specificity."; RL Biochemistry 36:6502-6510(1997). 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 -!- SIMILARITY: Belongs to the beta-eliminating lyase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X66978; CAA47388.1; -; Genomic_DNA. DR EMBL; L10821; AAA23098.1; -; Genomic_DNA. DR PIR; A49493; A49493. DR RefSeq; WP_003837154.1; NZ_VWTQ01000005.1. DR PDB; 1TPL; X-ray; 2.30 A; A/B=1-456. DR PDB; 2EZ1; X-ray; 1.90 A; A/B=1-456. DR PDB; 2EZ2; X-ray; 1.85 A; A/B=1-456. DR PDB; 2TPL; X-ray; 2.50 A; A/B=1-456. DR PDB; 2VLF; X-ray; 1.89 A; A/B=1-456. DR PDB; 2VLH; X-ray; 1.95 A; A/B=1-456. DR PDB; 2YCN; X-ray; 2.04 A; A/B=1-456. DR PDB; 2YCP; X-ray; 2.00 A; A/B/C/D=1-456. DR PDB; 2YCT; X-ray; 2.25 A; A/B=1-456. DR PDB; 2YHK; X-ray; 1.91 A; A/B=1-456. DR PDB; 6DUR; X-ray; 1.80 A; A/B=2-456. DR PDB; 6DVX; X-ray; 2.27 A; A/B=1-456. DR PDB; 6DXV; X-ray; 2.20 A; A/B=2-456. DR PDB; 6DYT; X-ray; 2.05 A; A/B=1-456. DR PDB; 6DZ5; X-ray; 2.26 A; A/B=1-456. DR PDB; 6ECG; X-ray; 2.27 A; A/B=2-456. DR PDB; 6MLS; X-ray; 1.77 A; A/B=1-456. DR PDB; 6MME; X-ray; 1.90 A; A/B=1-456. DR PDB; 6MO3; X-ray; 1.79 A; A/B=1-456. DR PDB; 6MPD; X-ray; 1.79 A; A/B=1-456. DR PDB; 6MQQ; X-ray; 2.05 A; A/B=2-456. DR PDB; 6NV8; X-ray; 2.26 A; A/B=1-456. DR PDB; 7TCS; X-ray; 1.37 A; A/B/C/D=1-456. DR PDB; 7TDL; X-ray; 1.60 A; A/B/C/D=1-456. DR PDBsum; 1TPL; -. DR PDBsum; 2EZ1; -. DR PDBsum; 2EZ2; -. DR PDBsum; 2TPL; -. DR PDBsum; 2VLF; -. DR PDBsum; 2VLH; -. DR PDBsum; 2YCN; -. DR PDBsum; 2YCP; -. DR PDBsum; 2YCT; -. DR PDBsum; 2YHK; -. DR PDBsum; 6DUR; -. DR PDBsum; 6DVX; -. DR PDBsum; 6DXV; -. DR PDBsum; 6DYT; -. DR PDBsum; 6DZ5; -. DR PDBsum; 6ECG; -. DR PDBsum; 6MLS; -. DR PDBsum; 6MME; -. DR PDBsum; 6MO3; -. DR PDBsum; 6MPD; -. DR PDBsum; 6MQQ; -. DR PDBsum; 6NV8; -. DR PDBsum; 7TCS; -. DR PDBsum; 7TDL; -. DR AlphaFoldDB; P31013; -. DR SMR; P31013; -. DR STRING; 1333848.CFNIH1_09255; -. DR DrugBank; DB03897; Phloretic acid. DR GeneID; 83644889; -. DR BRENDA; 4.1.99.2; 1398. DR EvolutionaryTrace; P31013; -. DR GO; GO:0050371; F:tyrosine phenol-lyase activity; IDA:CACAO. 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; IPR018176; Tryptophanase_CS. 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. DR PROSITE; PS00853; BETA_ELIM_LYASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Lyase; Pyridoxal phosphate. FT CHAIN 1..456 FT /note="Tyrosine phenol-lyase" FT /id="PRO_0000195631" FT MOD_RES 257 FT /note="N6-(pyridoxal phosphate)lysine" FT CONFLICT 205 FT /note="E -> A (in Ref. 2; AAA23098)" FT /evidence="ECO:0000305" FT STRAND 7..15 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 21..30 FT /evidence="ECO:0007829|PDB:7TCS" FT TURN 31..33 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 35..37 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 40..42 FT /evidence="ECO:0007829|PDB:7TCS" FT STRAND 44..46 FT /evidence="ECO:0007829|PDB:7TCS" FT STRAND 50..52 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 58..64 FT /evidence="ECO:0007829|PDB:7TCS" FT STRAND 71..73 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 75..88 FT /evidence="ECO:0007829|PDB:7TCS" FT STRAND 91..98 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 99..110 FT /evidence="ECO:0007829|PDB:7TCS" FT STRAND 116..121 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 124..132 FT /evidence="ECO:0007829|PDB:7TCS" FT STRAND 136..139 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 143..146 FT /evidence="ECO:0007829|PDB:7TCS" FT TURN 153..156 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 160..170 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 172..174 FT /evidence="ECO:0007829|PDB:7TCS" FT STRAND 175..184 FT /evidence="ECO:0007829|PDB:7TCS" FT TURN 185..188 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 194..206 FT /evidence="ECO:0007829|PDB:7TCS" FT STRAND 211..214 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 218..228 FT /evidence="ECO:0007829|PDB:7TCS" FT STRAND 233..235 FT /evidence="ECO:0007829|PDB:6DXV" FT HELIX 237..246 FT /evidence="ECO:0007829|PDB:7TCS" FT STRAND 249..254 FT /evidence="ECO:0007829|PDB:7TCS" FT TURN 255..259 FT /evidence="ECO:0007829|PDB:7TCS" FT STRAND 265..270 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 272..285 FT /evidence="ECO:0007829|PDB:7TCS" FT TURN 289..293 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 296..308 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 312..331 FT /evidence="ECO:0007829|PDB:7TCS" FT STRAND 342..348 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 349..352 FT /evidence="ECO:0007829|PDB:7TCS" FT TURN 353..355 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 358..360 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 362..374 FT /evidence="ECO:0007829|PDB:7TCS" FT STRAND 375..377 FT /evidence="ECO:0007829|PDB:7TCS" FT STRAND 379..382 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 383..386 FT /evidence="ECO:0007829|PDB:7TCS" FT TURN 390..392 FT /evidence="ECO:0007829|PDB:7TCS" FT STRAND 402..406 FT /evidence="ECO:0007829|PDB:7TCS" FT TURN 409..411 FT /evidence="ECO:0007829|PDB:6MLS" FT HELIX 414..428 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 429..433 FT /evidence="ECO:0007829|PDB:7TCS" FT STRAND 437..441 FT /evidence="ECO:0007829|PDB:7TCS" FT STRAND 444..446 FT /evidence="ECO:0007829|PDB:7TCS" FT HELIX 447..449 FT /evidence="ECO:0007829|PDB:7TCS" FT STRAND 452..455 FT /evidence="ECO:0007829|PDB:7TCS" SQ SEQUENCE 456 AA; 51500 MW; B77AB58233C22474 CRC64; MNYPAEPFRI KSVETVSMIP RDERLKKMQE AGYNTFLLNS KDIYIDLLTD SGTNAMSDKQ WAGMMMGDEA YAGSENFYHL ERTVQELFGF KHIVPTHQGR GAENLLSQLA IKPGQYVAGN MYFTTTRYHQ EKNGAVFVDI VRDEAHDAGL NIAFKGDIDL KKLQKLIDEK GAENIAYICL AVTVNLAGGQ PVSMANMRAV RELTEAHGIK VFYDATRCVE NAYFIKEQEQ GFENKSIAEI VHEMFSYADG CTMSGKKDCL VNIGGFLCMN DDEMFSSAKE LVVVYEGMPS YGGLAGRDME AMAIGLREAM QYEYIEHRVK QVRYLGDKLK AAGVPIVEPV GGHAVFLDAR RFCEHLTQDE FPAQSLAASI YVETGVRSME RGIISAGRNN VTGEHHRPKL ETVRLTIPRR VYTYAHMDVV ADGIIKLYQH KEDIRGLKFI YEPKQLRFFT ARFDYI //