ID A0A0F5ZV63_9GAMM Unreviewed; 488 AA.
AC A0A0F5ZV63;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
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:KKD59212.1};
GN ORFNames=RN22_17140 {ECO:0000313|EMBL:KKD59212.1};
OS Grimontia sp. AD028.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Grimontia.
OX NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD59212.1, ECO:0000313|Proteomes:UP000033732};
RN [1] {ECO:0000313|EMBL:KKD59212.1, ECO:0000313|Proteomes:UP000033732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD028 {ECO:0000313|EMBL:KKD59212.1,
RC ECO:0000313|Proteomes:UP000033732};
RA Adrian T.-G.-S., Chan K.-G.;
RT "Genome sequencing of Grimontia sp. AD028.";
RL Submitted (APR-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|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:KKD59212.1}.
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DR EMBL; LASY01000077; KKD59212.1; -; Genomic_DNA.
DR RefSeq; WP_046306107.1; NZ_LASY01000077.1.
DR AlphaFoldDB; A0A0F5ZV63; -.
DR PATRIC; fig|1581149.3.peg.4350; -.
DR OrthoDB; 9764079at2; -.
DR UniPathway; UPA00332; UER00452.
DR Proteomes; UP000033732; 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 InterPro; IPR018176; Tryptophanase_CS.
DR NCBIfam; TIGR02617; tnaA_trp_ase; 1.
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:KKD59212.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00544};
KW Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079, ECO:0000256|HAMAP-
KW Rule:MF_00544}.
FT DOMAIN 49..436
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 270
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00544,
FT ECO:0000256|PIRSR:PIRSR611166-50"
SQ SEQUENCE 488 AA; 54224 MW; 42D45955C9900D76 CRC64;
MENFKHLPEP FRIRVIEPVK RTTRVYREEA ILKAGMNPFL LDSEDVFIDL LTDSGTGAIT
QEMQAAMLRG DEAYSGSRSY YALSNAVKDI FGYDLTIPTH QGRGAEQIYI PVLIKKRELE
KGLDRSKMVA LSNYFFDTTQ GHTQVNCCVA KNIYTKDAFD TSVTADFKGN FDLQKLEAAI
LDAGAANVPY IVSTITCNSA GGQPVSIANL KAVYEIAKRY DIPVIMDSAR FAENAYFVQQ
REPGFKDWTI AEITREAYKY ADGLAMSAKK DAMVQMGGLL CFKDDAFMDV YQECRTLCVV
QEGFPTYGGL EGGAMERLAV GLYDGMRQEW LEYRIKQVQY LVDGLEAIGI VCQQAGGHAA
FVDAGKLLPH IPSDQFPAHA LACELYKVAG IRAVEIGSLL LGRDPATGKQ HPCPAELLRL
TIPRATYTQS HMDFIIEAFG EVKKNAHNVK GLDFTYEPSV LRHFTARLKE VEPAEVKKHN
AAELETTV
//
