ID A0A0J5GJ19_9NEIS Unreviewed; 462 AA.
AC A0A0J5GJ19;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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:KMJ54098.1};
GN ORFNames=ACG97_04650 {ECO:0000313|EMBL:KMJ54098.1};
OS Vogesella sp. EB.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Vogesella.
OX NCBI_TaxID=1526735 {ECO:0000313|EMBL:KMJ54098.1, ECO:0000313|Proteomes:UP000054352};
RN [1] {ECO:0000313|EMBL:KMJ54098.1, ECO:0000313|Proteomes:UP000054352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB {ECO:0000313|EMBL:KMJ54098.1,
RC ECO:0000313|Proteomes:UP000054352};
RA Arrua Day P., Revale S., Alvarez H.M.;
RT "Genome wide analysis of metabolism in the polyhydroxybutyrate-producing
RT Vogesella sp. strain EB.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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|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:KMJ54098.1}.
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DR EMBL; LFDT01000005; KMJ54098.1; -; Genomic_DNA.
DR RefSeq; WP_047966169.1; NZ_LFDT01000005.1.
DR AlphaFoldDB; A0A0J5GJ19; -.
DR STRING; 1526735.ACG97_04650; -.
DR PATRIC; fig|1526735.3.peg.994; -.
DR OrthoDB; 9764079at2; -.
DR UniPathway; UPA00332; UER00452.
DR Proteomes; UP000054352; Unassembled WGS sequence.
DR GO; GO:0009034; F:tryptophanase activity; IEA:UniProtKB-UniRule.
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 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:0000256|HAMAP-Rule:MF_00544, ECO:0000313|EMBL:KMJ54098.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00544}; Reference proteome {ECO:0000313|Proteomes:UP000054352};
KW Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079, ECO:0000256|HAMAP-
KW Rule:MF_00544}.
FT DOMAIN 47..428
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 262
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00544,
FT ECO:0000256|PIRSR:PIRSR611166-50"
SQ SEQUENCE 462 AA; 50736 MW; BB5ACA4F7FBFD856 CRC64;
MARRIPEPFR IKMVEPIKQT TPEFRRQALA EAGWNPFLLR GEDVYIDLLT DSGTGAMSDR
QWAGIMTGDE AYAGSRNYYQ LADTVKEVFG YQHTLPTHQG RGAEQILFPE LVKRCQGTQP
VFLSNYHFDT TKAHVEIAGA RAINVLTPKA LDTTTPYDWK GDFDLPRLAA TIEEVGAANV
AGLIVTVTCN SAGGQPVSMA SIREAAALAR QHGISVIIDA ARFAENAWFI QQRDPDYAGV
PVPAIVREMF SHGDMFTMSS KKDALVNIGG LCCFKDDIEL FRTVQVRCVA MEGFITYGGL
AGRDMAAMAI GLREGMDEDY LAYRIGQVAY LGERLAAGGI PIQTPTGGHA VFVDAKKLLP
HIPAEQFPAH ALACELYLEG GIRGVEIGSL LLGRNPATGE QETSPFELLR LTIPRRVYTN
DHMDYIADCL IDIQSRAAGI RGLAFDYEPP ILRHFTARLK PV
//
