ID A0A1G0X6P3_9BACT Unreviewed; 457 AA.
AC A0A1G0X6P3;
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:OGV29394.1};
GN ORFNames=A2523_08735 {ECO:0000313|EMBL:OGV29394.1};
OS Ignavibacteria bacterium RIFOXYD12_FULL_36_8.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798454 {ECO:0000313|EMBL:OGV29394.1, ECO:0000313|Proteomes:UP000177243};
RN [1] {ECO:0000313|EMBL:OGV29394.1, ECO:0000313|Proteomes:UP000177243}
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:OGV29394.1}.
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DR EMBL; MHBA01000094; OGV29394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0X6P3; -.
DR STRING; 1798454.A2523_08735; -.
DR Proteomes; UP000177243; 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 InterPro; IPR018176; Tryptophanase_CS.
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.
DR PROSITE; PS00853; BETA_ELIM_LYASE; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:OGV29394.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR611166-50}.
FT DOMAIN 46..421
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 257
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611166-50"
SQ SEQUENCE 457 AA; 51175 MW; BD50B13D292A0022 CRC64;
MKTIIEPFKI KSVEPIRFTT KEERIKLIKK AGYNPFLLHA DDVLIDLLTD SGTSAMSSKQ
WAGIMDGDES YAGSKSFYRF EDAVKKITGM KFIIPTHQGR AAEKILFSIV GGKGKYFPNN
THFDTTRANI EFTGAEADDF IVEVGKHSEV RADFKGNMDT ALLKKFIEEK GSENIPLCMI
TVTNNSGGGQ PVSMQNIKEV KDICVNYNIP LFIDACRFAE NAYFIKLREK GYSKKSVLEI
AQEMFSYADG ATMSAKKDAL VNIGGFLALN DKNLAMQCRN LLIVTEGFPT YGGLAGRDLE
AVAQGLKEIL DEHYLQYRIR SVAYLGEKLV AAGVPIIEPP GGHAIYIDAK RFLPNIPPEN
YPGQSIVCEL YIEGGIRAVE IGSVMFGKYN ENGKLIPPPM ELVRLAVPRR VYTQSHIDYV
IEIILEVFRN RNKLNGYKIT YEAPMLKHFT ARFEKIK
//
