ID G9ZJ18_9GAMM Unreviewed; 472 AA.
AC G9ZJ18;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 65.
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=HMPREF9080_02787 {ECO:0000313|EMBL:EHM50598.1};
OS Cardiobacterium valvarum F0432.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Cardiobacteriaceae; Cardiobacterium.
OX NCBI_TaxID=797473 {ECO:0000313|EMBL:EHM50598.1, ECO:0000313|Proteomes:UP000004750};
RN [1] {ECO:0000313|EMBL:EHM50598.1, ECO:0000313|Proteomes:UP000004750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0432 {ECO:0000313|EMBL:EHM50598.1,
RC ECO:0000313|Proteomes:UP000004750};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) 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:EHM50598.1}.
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DR EMBL; AGCM01000178; EHM50598.1; -; Genomic_DNA.
DR RefSeq; WP_006986771.1; NZ_JH417966.1.
DR AlphaFoldDB; G9ZJ18; -.
DR STRING; 797473.HMPREF9080_02787; -.
DR PATRIC; fig|797473.3.peg.2267; -.
DR HOGENOM; CLU_047223_0_0_6; -.
DR UniPathway; UPA00332; UER00452.
DR Proteomes; UP000004750; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
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 Dioxygenase {ECO:0000313|EMBL:EHM50598.1};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00544};
KW Oxidoreductase {ECO:0000313|EMBL:EHM50598.1};
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..437
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 472 AA; 52755 MW; AFE22B1E1883C654 CRC64;
MENFTHIPEP FRIRVIEPVK RTTREYREKA IIKAGMNPFL LDSEDVFIDL LTDSGTGAVT
QDMQAAMLRG DEAYSGSRSY YALARAVKEI FGYDYTIPTH QGRGAEQIYI PVLIKKREQE
KGLDRSKMVA FSNYFFDTTQ GHSQINGCTV RNVYTKEAFD TSVKSDFKGN FDLEKLEAGI
QEVGAANVPY IVCTITCNSA GGQPVSIANL RGMYAVAQKY DIPVVMDSAR FAENAYFIQQ
REPGYKDKSI EEITFESYQY ADMLAMSAKK DAMVPMGGLL CVKNERYQDV YTECRTLCVV
QEGFPTYGGL EGGAMERLAV GLRDGMRQDW LAYRIGQVEY LVNRLEAIGV VCQQPGGHAA
FVDAGKLLPH IPQEQFPAQA LACELYKVAG IRAVEIGSFL QGRDPKTGKQ LPCPAELLRL
TIPRATYTQS HMDFIVEAFK QVKANAPKIK GLTFTYEPKV LRHFTALLKE VG
//
