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Database: UniProt
Entry: A0A1F8SWE6_9CHLR
LinkDB: A0A1F8SWE6_9CHLR
Original site: A0A1F8SWE6_9CHLR 
ID   A0A1F8SWE6_9CHLR        Unreviewed;       462 AA.
AC   A0A1F8SWE6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Tyrosine phenol-lyase {ECO:0000313|EMBL:OGO64229.1};
GN   ORFNames=A2Z45_11210 {ECO:0000313|EMBL:OGO64229.1};
OS   Chloroflexi bacterium RBG_19FT_COMBO_55_16.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797669 {ECO:0000313|EMBL:OGO64229.1, ECO:0000313|Proteomes:UP000177674};
RN   [1] {ECO:0000313|EMBL:OGO64229.1, ECO:0000313|Proteomes:UP000177674}
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR611166-50};
CC   -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC       {ECO:0000256|ARBA:ARBA00009721}.
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:OGO64229.1}.
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DR   EMBL; MGOK01000091; OGO64229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8SWE6; -.
DR   STRING; 1797669.A2Z45_11210; -.
DR   Proteomes; UP000177674; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0009072; P:aromatic amino acid 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   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   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:0000313|EMBL:OGO64229.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR611166-50}.
FT   DOMAIN          47..424
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         258
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611166-50"
SQ   SEQUENCE   462 AA;  51569 MW;  B0F03A1565089CB0 CRC64;
     MVSYPPEPFR IKMVEPIQQV DRQQRTESLR RAGYNLFGLR SDEIFIDLLT DSGTGAMSQA
     QWAALMLGDE SYAGARSFFH LAEAIHDIFG FRFFTPTHQG RAAENILCAL MVKEGQYVPS
     NMHFDTTDAN IRARGGHPTN LVIAAAYEPS NRHPFKGNMD VQKLENFIAE VGVDRIPLGM
     ITITNNAGGG QPVSLENIRT VAQIYHAHGI PFFIDACRYA ENAYFIKERE PGYVDKSPLE
     IARQIFALAD GATMSAKKDA IVNIGGFLAM NDEDLYRRAC NELILREGFP TYGGLAGRDL
     DAIAVGLREG LDENYLAYRL GQTAYLAERL LELGIPIIEP PGGHAVYLDA GRLLPHIPQK
     EFPGQALAVE LYLEGGIRAV EIGSVMFAHP DPETNELTYP KLELVRLAIP RRVYTQSHLD
     YVAETLAVIA KHKEDVRGYR FTYAPPLLRH FTARFEPLSN QR
//
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