ID G9WYQ3_9FIRM Unreviewed; 460 AA.
AC G9WYQ3; G9XBA7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 ORFNames=HMPREF9628_01274 {ECO:0000313|EMBL:EHL19758.1},
GN HMPREF9629_01304 {ECO:0000313|EMBL:EHL16235.1};
OS Peptoanaerobacter stomatis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptoanaerobacter.
OX NCBI_TaxID=796937 {ECO:0000313|EMBL:EHL16235.1, ECO:0000313|Proteomes:UP000006437};
RN [1] {ECO:0000313|EMBL:EHL16235.1, ECO:0000313|Proteomes:UP000006437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACC19a {ECO:0000313|EMBL:EHL16235.1,
RC ECO:0000313|Proteomes:UP000006437};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Sizova M., Hazen A.,
RA Epstein S., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Eubacteriaceae bacterium ACC19a.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EHL19758.1, ECO:0000313|Proteomes:UP000003379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM5 {ECO:0000313|EMBL:EHL19758.1,
RC ECO:0000313|Proteomes:UP000003379};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Sizova M., Hazen A.,
RA Epstein S., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Eubacteriaceae bacterium CM5.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHL16235.1}.
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DR EMBL; AFZE01000004; EHL16235.1; -; Genomic_DNA.
DR EMBL; AFZG01000015; EHL19758.1; -; Genomic_DNA.
DR RefSeq; WP_009525537.1; NZ_JH414605.1.
DR AlphaFoldDB; G9WYQ3; -.
DR STRING; 796937.HMPREF9630_00639; -.
DR PATRIC; fig|796937.3.peg.497; -.
DR HOGENOM; CLU_047223_0_0_9; -.
DR Proteomes; UP000003379; Unassembled WGS sequence.
DR Proteomes; UP000006437; Unassembled WGS sequence.
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:EHL16235.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00543}.
FT DOMAIN 49..425
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 260
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00543,
FT ECO:0000256|PIRSR:PIRSR611166-50"
SQ SEQUENCE 460 AA; 51805 MW; 741F8737E401130A CRC64;
MDFSKYPAEP FKIKVVEPVK MISKEERIAA IKEAGYNTFN LKSEDCYIDL LTDSGTNAMS
DSQWAGMMIG DEAYAGSKNW VFLESTIKEL FGFKHVVPTH QGRGAENILS TIAIKPGQYV
LGNMYFTTTR YHQERNGGIF MDIIRQEAHD ATIDIPFKGD IDVEKMESII KEKGPENIAY
VCLAVTVNLA GGQPVSMKNM KEVRKVADKY GVKVFYDATR CVENAYFIKE QEEGYQDKTI
KEICHEMFSY SDGATCSGKK DGIVNIGGFL AINDDELFGK AKEIVVVFEG MPSYGGMSGR
DMQAIAIGFR EAMQFEYIEH RVKQVRYLGD RLKEAGIPIV EPVGGHAVFL DARRFCPHLN
QEQFPAQSLA AALYVEAGVR SMERGIVSAG RDAKTGENHK PKLETVRLTI PRRVYTYAHM
DIVAEACIKL FKHKEDIKPL KFVYEPKQLR FFTAKFDIAE
//
