TPL_FUSNN
ID TPL_FUSNN Reviewed; 460 AA.
AC Q8RHM6;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=FN1988;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
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; AE009951; AAL94078.1; -; Genomic_DNA.
DR RefSeq; NP_602779.1; NC_003454.1.
DR AlphaFoldDB; Q8RHM6; -.
DR SMR; Q8RHM6; -.
DR STRING; 190304.FN1988; -.
DR PRIDE; Q8RHM6; -.
DR EnsemblBacteria; AAL94078; AAL94078; FN1988.
DR KEGG; fnu:FN1988; -.
DR PATRIC; fig|190304.8.peg.456; -.
DR eggNOG; COG3033; Bacteria.
DR HOGENOM; CLU_047223_0_0_0; -.
DR InParanoid; Q8RHM6; -.
DR OMA; EMYQYGD; -.
DR BioCyc; FNUC190304:G1FZS-478-MON; -.
DR BRENDA; 4.1.99.2; 11865.
DR Proteomes; UP000002521; 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; 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 3: Inferred from homology;
KW Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..460
FT /note="Tyrosine phenol-lyase"
FT /id="PRO_0000195635"
FT MOD_RES 260
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00543"
SQ SEQUENCE 460 AA; 52156 MW; 477A4690F7EA1D32 CRC64;
MRFEDYPAEP FRIKSVETVK MIDKAAREEV IKKAGYNTFL INSEDVYIDL LTDSGTNAMS
DKQWGGLMQG DEAYAGSRNF FHLEETVKEI FGFKHIVPTH QGRGAENILS QIAIKPGQYV
PGNMYFTTTR YHQERNGGIF KDIIRDEAHD ATLNVPFKGD IDLNKLQKLI DEVGAENIAY
VCLAVTVNLA GGQPVSMKNM KAVRELTKKH GIKVFYDATR CVENAYFIKE QEEGYQDKTI
KEIVHEMFSY ADGCTMSGKK DCLVNIGGFL CMNDEDLFLA AKEIVVVYEG MPSYGGLAGR
DMEAMAIGLR ESLQYEYIRH RILQVRYLGE KLKEAGVPIL EPVGGHAVFL DARRFCPHIP
QEEFPAQALA AAIYVECGVR TMERGIISAG RDVKTGENHK PKLETVRVTI PRRVYTYKHM
DVVAEGIIKL YKHKEDIKPL EFVYEPKQLR FFTARFGIKK