ID A0A1G0WD90_9BACT Unreviewed; 461 AA.
AC A0A1G0WD90;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=A2475_04645 {ECO:0000313|EMBL:OGV19363.1};
OS Ignavibacteria bacterium RIFOXYC2_FULL_35_21.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798452 {ECO:0000313|EMBL:OGV19363.1, ECO:0000313|Proteomes:UP000177327};
RN [1] {ECO:0000313|EMBL:OGV19363.1, ECO:0000313|Proteomes:UP000177327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV19363.1}.
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DR EMBL; MHAY01000091; OGV19363.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0WD90; -.
DR STRING; 1798452.A2475_04645; -.
DR Proteomes; UP000177327; 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:OGV19363.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00543}.
FT DOMAIN 50..424
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 261
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00543,
FT ECO:0000256|PIRSR:PIRSR611166-50"
SQ SEQUENCE 461 AA; 52504 MW; 200165E510C84CCE CRC64;
MPNYRKPWAE PYKIKVVEPL KVTTREYREE KMKEAGYNTF LLRSVDVYID LLTDSGTTAM
SDYQWAGMML GDEAYAGSKN FYYLEDNVKK YYGYKHMVPT HQGRAAEHLL SRVMIKQGDY
VPGNMYFTTT RLHQELAGGT FVDVIIDEAH DPANKHPFKG NVDLQKVEDL IKKVGANKIP
YICVAGTVNM AGGQPQSMEN MKALRKLADK HGLKIMLDAT RAVENAYFVK DREAGYANKT
IEEILLEYCS LSDGCTMSGK KDLLVNIGGF VAVNDEHLFD ELRNLVVVYE GLHTYGGLAG
RDMEAMARGI KECVNYDHIR SRVEQVRYFG QKLLDAGVPI VEPAGGHAIF LDAKRFYEHI
PQEQLPAQAL AADLYIESGV RAMERGIVSA GRNKETGEHN FPKLELVRLT FPRRVYTQAH
LDVAAWHVED LYEKRHNAKG LKFIYEPQYL RFFQAKFERL D
//
