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Database: UniProt
Entry: A0A0S7WII0_9CHLR
LinkDB: A0A0S7WII0_9CHLR
Original site: A0A0S7WII0_9CHLR 
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}.
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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
//
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