ID K8WIB5_9GAMM Unreviewed; 467 AA.
AC K8WIB5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Tryptophanase {ECO:0000256|HAMAP-Rule:MF_00544};
DE EC=4.1.99.1 {ECO:0000256|HAMAP-Rule:MF_00544};
DE AltName: Full=L-tryptophan indole-lyase {ECO:0000256|HAMAP-Rule:MF_00544};
DE Short=TNase {ECO:0000256|HAMAP-Rule:MF_00544};
GN Name=tnaA {ECO:0000256|HAMAP-Rule:MF_00544,
GN ECO:0000313|EMBL:EKT55945.1};
GN ORFNames=OO7_13289 {ECO:0000313|EMBL:EKT55945.1};
OS Providencia sneebia DSM 19967.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1141660 {ECO:0000313|EMBL:EKT55945.1, ECO:0000313|Proteomes:UP000010290};
RN [1] {ECO:0000313|EMBL:EKT55945.1, ECO:0000313|Proteomes:UP000010290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19967 {ECO:0000313|EMBL:EKT55945.1,
RC ECO:0000313|Proteomes:UP000010290};
RX PubMed=23145767; DOI=10.1186/1471-2164-13-612;
RA Galac M.R., Lazzaro B.P.;
RT "Comparative genomics of bacteria in the genus Providencia isolated from
RT wild Drosophila melanogaster.";
RL BMC Genomics 13:612-612(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-tryptophan = indole + NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:19553, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16881, ChEBI:CHEBI:28938, ChEBI:CHEBI:57912; EC=4.1.99.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001826, ECO:0000256|HAMAP-
CC Rule:MF_00544};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00544, ECO:0000256|PIRSR:PIRSR611166-50};
CC -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via pyruvate
CC pathway; indole and pyruvate from L-tryptophan: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004662, ECO:0000256|HAMAP-Rule:MF_00544}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|HAMAP-Rule:MF_00544}.
CC -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC {ECO:0000256|ARBA:ARBA00009721, ECO:0000256|HAMAP-Rule:MF_00544}.
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:EKT55945.1}.
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DR EMBL; AKKN01000010; EKT55945.1; -; Genomic_DNA.
DR RefSeq; WP_008916411.1; NZ_CM001773.1.
DR AlphaFoldDB; K8WIB5; -.
DR PATRIC; fig|1141660.3.peg.2655; -.
DR HOGENOM; CLU_047223_0_0_6; -.
DR OrthoDB; 9764079at2; -.
DR UniPathway; UPA00332; UER00452.
DR Proteomes; UP000010290; Chromosome.
DR GO; GO:0009034; F:tryptophanase activity; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00544; Tryptophanase; 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; IPR013440; TNase.
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:0000256|HAMAP-Rule:MF_00544, ECO:0000313|EMBL:EKT55945.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00544}; Reference proteome {ECO:0000313|Proteomes:UP000010290};
KW Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079, ECO:0000256|HAMAP-
KW Rule:MF_00544}.
FT DOMAIN 47..432
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|HAMAP-Rule:MF_00544,
FT ECO:0000256|PIRSR:PIRSR611166-50"
SQ SEQUENCE 467 AA; 52582 MW; 917261B758D75D27 CRC64;
MAKRIVEPFR IKMVENIRIP SREEREIALK EAGYNPFLLP SSAVYIDLLT DSGTNAMSDH
QWAAMITGDE AYAGSRNYYD LQNKVKEMFG YEYTIPAHQG RGVENMLFPV LLKVKQEQGG
AKNPVFISNF HFDTTAAHVE LNGCKAINIV TEKAYDSETY DDWKGNFDIQ KLKDNIAKYG
AENVVAIVST VTCNSAGGQP VSMENLKEVY EIAKQHNIFV VMDSARFCEN AYFIKERDPK
YKDATIKEII FDMYKYADAL TMSAKKDPLL NIGGLVAIKD DEHIFTLARQ RCVPMEGFVT
YGGLAGRDMA AMVQGLEEGA NEDYLHYRIG QVKYLGDRLR EAGIPIQYPT GGHAVFVDCK
KLVPQIPGDQ FPAQAVINAL YLESGVRAVE IGSFLLGRDP ETGKQKHADM EFMRLTIARR
VYTNDHMDYI ADALIGLKDK FATLKGLDFE YEPPVLRHFT ARLKPIK
//
