ID A0A0S7WII0_9CHLR Unreviewed; 462 AA.
AC A0A0S7WII0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Tryptophanase {ECO:0000313|EMBL:KPJ49988.1};
GN ORFNames=AMJ38_02500 {ECO:0000313|EMBL:KPJ49988.1};
OS Dehalococcoidia bacterium DG_22.
OC Bacteria; Chloroflexota; Dehalococcoidia.
OX NCBI_TaxID=1703393 {ECO:0000313|EMBL:KPJ49988.1, ECO:0000313|Proteomes:UP000054105};
RN [1] {ECO:0000313|EMBL:KPJ49988.1, ECO:0000313|Proteomes:UP000054105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_22 {ECO:0000313|EMBL:KPJ49988.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ49988.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LIZQ01000044; KPJ49988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7WII0; -.
DR PATRIC; fig|1703393.3.peg.394; -.
DR Proteomes; UP000054105; 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 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR611166-50}.
FT DOMAIN 49..424
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|PIRSR:PIRSR611166-50"
SQ SEQUENCE 462 AA; 51512 MW; 9B33930A4F344444 CRC64;
MANVGIMPEP YRIKVVEPIR LNSYEERTRI LEAAGYNLFM VPAEEVFIDL LTDSGTSAMS
IHQWAGVMQG DESYAGSRSY FRFENAIKDI MGFKYVLPTH QGRGGDRILF GIFARPGKAI
PSNMHFDSSR GHTESRGGRA MDLVIDEAYD PRNLCPFKGN MDLAKLESFI SETGAENIPM
ILMTVHNNVG GGQPISLENI RGTKEIASRY GIPLFIDAAR FAENAYFIKE REHGYADKSI
PEIVKEMMSY FDGCTMSAKK DGLANIGGFL AMNDHDLWLR CAPRIVANEG FIHYGGMSGR
DLEAIARGLY EVMDEAYLAN RIRQVRYLGE RLVEAGIEVI QPIGGHGVFV DAKAFLPHVP
QEQLTADALA VAVYQECGVR GAALGTLWAE RDPVTGKDRP PKLELYRLAV PRRVYTDRHM
DYVAQGIREV FANREKVSGL EIVYEPRGAR SFLARLKPIG QS
//