ID A0A0K8QSD3_9BACT Unreviewed; 487 AA.
AC A0A0K8QSD3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Tryptophanase {ECO:0000313|EMBL:GAP67849.1};
GN ORFNames=BA6E_101295 {ECO:0000313|EMBL:GAP67849.1};
OS Bacteroidales bacterium 6E.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1688776 {ECO:0000313|EMBL:GAP67849.1, ECO:0000313|Proteomes:UP000251980};
RN [1] {ECO:0000313|Proteomes:UP000251980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6E {ECO:0000313|Proteomes:UP000251980};
RA Tourlousse D.M., Honda T., Matsuura N., Ohashi A., Tonouchi A.,
RA Sekiguchi Y.;
RT "Draft Genome Sequence of Bacteroidales Strain 6E, Isolated from a Rice
RT Paddy Field in Japan.";
RL Genome Announc. 3:e01167-e01115(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}.
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DR EMBL; DF970666; GAP67849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K8QSD3; -.
DR STRING; 1688776.GCA_001270045_00295; -.
DR OrthoDB; 9764079at2; -.
DR Proteomes; UP000251980; 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 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR611166-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000251980}.
FT DOMAIN 60..431
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 271
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611166-50"
SQ SEQUENCE 487 AA; 54552 MW; F3C321CD21131C51 CRC64;
MVQPTLTEVK FSNGAKIPVE LHKVRVVQKL HLKPVDERLA AMAAGGYNTF QLNTRDIFLD
MLTDSGTNAM SDNQVSSMLH ADDAYAGSQS FYRMEKAVQH VFGKKWVLPV HQGRAAENII
SQAFISKGHV IPMNYHFTTT MAHMELNGGK VFEIYTDEAL KIKSDNQFKG NIDINKLQAL
IDQYGPERIP FIRMEASTNL IGGQPFSIQN MREVRAIADK YGIMVVLDAS LIGENAWFIK
KREEEFKNQS IHDILLTMCD LAQLVYFSSR KVSSTRGGGI ATNDESIFLK MRDLVVLYEG
FTTYGGISVR EIEAMAVGLY ETMDETVISQ SPSFIEYTVN ELDSLGVPVI MPAGALGCHI
DARGFLPHLP QSEYPAGALA AALFIVSGIR GMERGTISSV RDENGNDILA DVELLRLAFP
RRVFTLSQTM FVIDRVHWLY KNRELIGGLR FVDEPKVLRF FNGKLEPTSD WPQKLVAKFK
EDFGNSL
//