GenomeNet

Database: UniProt
Entry: A0A1C6LH23_9NEIS
LinkDB: A0A1C6LH23_9NEIS
Original site: A0A1C6LH23_9NEIS 
ID   A0A1C6LH23_9NEIS        Unreviewed;       462 AA.
AC   A0A1C6LH23;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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   ORFNames=PSELUDRAFT_0181 {ECO:0000313|EMBL:SCK05905.1};
OS   Vogesella sp. LIG4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Vogesella.
OX   NCBI_TaxID=1192162 {ECO:0000313|EMBL:SCK05905.1, ECO:0000313|Proteomes:UP000198213};
RN   [1] {ECO:0000313|EMBL:SCK05905.1, ECO:0000313|Proteomes:UP000198213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LIG4 {ECO:0000313|Proteomes:UP000198213};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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|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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LT607802; SCK05905.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6LH23; -.
DR   OrthoDB; 9764079at2; -.
DR   UniPathway; UPA00332; UER00452.
DR   Proteomes; UP000198213; Chromosome i.
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};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00544}; Reference proteome {ECO:0000313|Proteomes:UP000198213};
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;  50854 MW;  DD9354E83990B060 CRC64;
     MARRIPEPFR IKMVEPIKQT SGDYRRQALE TAGWNPFLLR GEDVYIDLLT DSGTGAMSDR
     QWAGIMSGDE AYAGSRNFYQ LADTVQEVFG YRHTLPTHQG RGAEQILFPE LVKRCQGDSP
     VFLSNYHFDT TKAHVEIAGA RAINVLTDKA LDTTTPYDWK GDFDLPRLAA TIEQVGAANV
     AGLIITVTCN SAGGQPVSMH SIRESAALAR KHGIPVVIDA ARFAENAWFI QQRDPDYAAM
     SVADIVREMF SHGDMFTMSA KKDALVNIGG LCCFKDDEAL FRRVQVRCVA MEGFITYGGL
     AGRDMAALAI GLKEGMDEGH LAYRIGQVAY LGDRLAAAGI PIQTPTGGHA VFVDARKLLP
     HIPAQQFPAH ALACELYIEG GIRGVEIGSL LLGRNPASGE QEPSPFELLR LTIPRRVYTN
     DHMDYIADCL IDIRERAGSI RGLTFEYEPP LLRHFTARLK PV
//
DBGET integrated database retrieval system