ID A0A1H5XQD8_9RHOO Unreviewed; 482 AA.
AC A0A1H5XQD8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Tryptophanase {ECO:0000313|EMBL:APR05321.1};
DE EC=4.1.99.1 {ECO:0000313|EMBL:APR05321.1};
GN ORFNames=SAMN05216242_11949 {ECO:0000313|EMBL:SEG13914.1}, Tchl_2494
GN {ECO:0000313|EMBL:APR05321.1};
OS Thauera chlorobenzoica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=96773 {ECO:0000313|EMBL:APR05321.1, ECO:0000313|Proteomes:UP000185739};
RN [1] {ECO:0000313|EMBL:SEG13914.1, ECO:0000313|Proteomes:UP000236741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3CB-1 {ECO:0000313|EMBL:SEG13914.1,
RC ECO:0000313|Proteomes:UP000236741};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:APR05321.1, ECO:0000313|Proteomes:UP000185739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3CB1 {ECO:0000313|EMBL:APR05321.1,
RC ECO:0000313|Proteomes:UP000185739};
RA Goris T., Mergelsberg M., Boll M.;
RT "Complete genome sequence of Thauera chlorobenzoica, a Betaproteobacterium
RT degrading haloaromatics anaerobically to CO2 and halides.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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; CP018839; APR05321.1; -; Genomic_DNA.
DR EMBL; FNVJ01000019; SEG13914.1; -; Genomic_DNA.
DR RefSeq; WP_075148694.1; NZ_FNVJ01000019.1.
DR AlphaFoldDB; A0A1H5XQD8; -.
DR STRING; 96773.Tchl_2494; -.
DR KEGG; tcl:Tchl_2494; -.
DR OrthoDB; 9764079at2; -.
DR Proteomes; UP000185739; Chromosome.
DR Proteomes; UP000236741; Unassembled WGS sequence.
DR GO; GO:0009034; F:tryptophanase activity; IEA:UniProtKB-EC.
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:APR05321.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR611166-50}.
FT DOMAIN 55..423
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 266
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611166-50"
SQ SEQUENCE 482 AA; 53658 MW; D072C1E7404AE2A5 CRC64;
MAKVKFYGGE SVPLEMHKVR IVQKLNLPPV ERRLEAITEA GNNTFLLRNA DVFMDMLTDS
GVNAMSDQQQ AAMMIADDSY AGSATYTRLE AKLQDIFGMD YFLPAHQGRA CENILGQVLV
TPGSVVPMNY HFTTTKAHIT LNGGIVEELV SDAGLEVVSV HPFKGNMDVA KLQAVIGKHG
ADKIAFVRME AGTNLIGGQP FSLENLADIR KVCDQHRLLL VLDASLLADN LHFIKNREES
CKALSIREIT RKMADLCDLI YFSARKLGCA RGGGMCMRSE ELYRRMRGLI PLYEGFLTYG
GMSVREMEAL TVGLEETMDE EVINQGPQFI GYMVDELQKR DIPVITPAGG LGCHINAMKF
VDHIPQAQYP AGALASALYI AGGIRGMERG TLSEQREPDG SEIFANMELV RLALPRRVFT
LSQVKYAVDR LEWLYANRRL IGGLVFTEEP EILRFFYGRL APVSNWQEKL VAKFREDFGD
SL
//
