TPL_CITFR
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 25-MAY-2022, entry version 129.
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; Proteobacteria; 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}.
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DR EMBL; X66978; CAA47388.1; -; Genomic_DNA.
DR EMBL; L10821; AAA23098.1; -; Genomic_DNA.
DR PIR; A49493; A49493.
DR RefSeq; WP_003837154.1; NZ_VKUV01000008.1.
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 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 AlphaFoldDB; P31013; -.
DR SMR; P31013; -.
DR STRING; 1333848.CFNIH1_09255; -.
DR DrugBank; DB03897; Phloretic acid.
DR GeneID; 60898220; -.
DR GeneID; 67518133; -.
DR OrthoDB; 91973at2; -.
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 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; 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:2YCP"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:6MLS"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:6MLS"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:6MLS"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:6MLS"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 75..88
FT /evidence="ECO:0007829|PDB:6MLS"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:6MLS"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:6MLS"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:6MLS"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:6MLS"
FT STRAND 175..184
FT /evidence="ECO:0007829|PDB:6MLS"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:6MLS"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:6MLS"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:6DXV"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:6MLS"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:6MLS"
FT TURN 255..259
FT /evidence="ECO:0007829|PDB:6MLS"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 272..285
FT /evidence="ECO:0007829|PDB:6MLS"
FT TURN 289..293
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 296..309
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 312..331
FT /evidence="ECO:0007829|PDB:6MLS"
FT STRAND 342..348
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:6MLS"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 362..374
FT /evidence="ECO:0007829|PDB:6MLS"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:6MLS"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:6MLS"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:6MLS"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:6MLS"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 414..428
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 429..433
FT /evidence="ECO:0007829|PDB:6MLS"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:6MLS"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:6MLS"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:6MLS"
FT STRAND 452..455
FT /evidence="ECO:0007829|PDB:6MLS"
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
