ID M1ZEE1_9FIRM Unreviewed; 460 AA.
AC M1ZEE1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 58.
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:SHD77497.1};
GN ORFNames=CUESP1_2143 {ECO:0000313|EMBL:SHD77497.1};
OS [Clostridium] ultunense Esp.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Tepidimicrobiaceae;
OC Schnuerera.
OX NCBI_TaxID=1288971 {ECO:0000313|EMBL:SHD77497.1, ECO:0000313|Proteomes:UP000245423};
RN [1] {ECO:0000313|EMBL:SHD77497.1, ECO:0000313|Proteomes:UP000245423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Clostridium ultunense strain Esp {ECO:0000313|EMBL:SHD77497.1};
RA Manzoor S.;
RL Submitted (NOV-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|HAMAP-Rule:MF_00544}.
CC -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC {ECO:0000256|ARBA:ARBA00009721, ECO:0000256|HAMAP-Rule:MF_00544}.
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DR EMBL; LT669839; SHD77497.1; -; Genomic_DNA.
DR AlphaFoldDB; M1ZEE1; -.
DR HOGENOM; CLU_047223_0_0_9; -.
DR OrthoDB; 9764079at2; -.
DR UniPathway; UPA00332; UER00452.
DR Proteomes; UP000245423; Chromosome chri.
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 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:SHD77497.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00544}; Reference proteome {ECO:0000313|Proteomes:UP000245423};
KW Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079, ECO:0000256|HAMAP-
KW Rule:MF_00544}.
FT DOMAIN 48..425
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 259
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00544,
FT ECO:0000256|PIRSR:PIRSR611166-50"
SQ SEQUENCE 460 AA; 51461 MW; 8A67BDD754B34FD7 CRC64;
MKSKYYAEPF KIKMVEPIKI LTAEERLEKI KEANYNLFSL DSEDVYIDLL SDSGTGAMST
GQWAGMMAGD EAYSGSKNFK NLERAAQNIF GYKYIQPVHQ GRAAEKVVLP ILLGPGKYAI
SNMHFDTTRA HVEIAGARAI DCVVPEALDT ETYSPFKGNM DTKRLKKLIA EYGAKNIGLI
IMTITNNSAG GQPVSMENLR ETSKIAAEYN IPLLIDAARF AENAYFIKQR EKGYEDKSIR
EIVLEMFSYG KIFTMSSKKD AIVNIGGLIG IKDDEGLYEE VKARTIPFEG FISYGGLAGR
DLEALAIGLE EGIDYNYLKY RIGQMEYLAA RLDKANIPYQ SPVGGHAVFI DAKKLLPHIP
YYEFPGQALA VELYKEAGIR TCDIGSFMMG NDPDTGEQIE SQFEFTRLAI PRRVYTQSHL
DVIADALMSI KERADSISGY KINWEPEILR HFTAKLVPKK
//
