ID TNAA_DESVH Reviewed; 462 AA.
AC Q729Z3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Tryptophanase {ECO:0000255|HAMAP-Rule:MF_00544};
DE EC=4.1.99.1 {ECO:0000255|HAMAP-Rule:MF_00544};
DE AltName: Full=L-tryptophan indole-lyase {ECO:0000255|HAMAP-Rule:MF_00544};
DE Short=TNase {ECO:0000255|HAMAP-Rule:MF_00544};
GN Name=tnaA {ECO:0000255|HAMAP-Rule:MF_00544}; OrderedLocusNames=DVU_2204;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Nitratidesulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
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:0000255|HAMAP-Rule:MF_00544};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00544};
CC -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via pyruvate
CC pathway; indole and pyruvate from L-tryptophan: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00544}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00544}.
CC -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC {ECO:0000255|HAMAP-Rule:MF_00544}.
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DR EMBL; AE017285; AAS96677.1; -; Genomic_DNA.
DR RefSeq; WP_010939479.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_011417.1; NC_002937.3.
DR AlphaFoldDB; Q729Z3; -.
DR SMR; Q729Z3; -.
DR STRING; 882.DVU_2204; -.
DR PaxDb; 882-DVU_2204; -.
DR EnsemblBacteria; AAS96677; AAS96677; DVU_2204.
DR KEGG; dvu:DVU_2204; -.
DR PATRIC; fig|882.5.peg.2003; -.
DR eggNOG; COG3033; Bacteria.
DR HOGENOM; CLU_047223_0_0_7; -.
DR OrthoDB; 9764079at2; -.
DR PhylomeDB; Q729Z3; -.
DR UniPathway; UPA00332; UER00452.
DR Proteomes; UP000002194; Chromosome.
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; Pyridoxal phosphate; Reference proteome; Tryptophan catabolism.
FT CHAIN 1..462
FT /note="Tryptophanase"
FT /id="PRO_1000061070"
FT MOD_RES 261
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00544"
SQ SEQUENCE 462 AA; 51358 MW; 4F5A78357E5E4C5C CRC64;
MKRIPEPFRI KMIEPIRMTT LEDRTRALEE AGYNPFLLKS EDVYIDLLTD SGTGAMSDRQ
WAGLMMGDEA YAGSRNFLNL EKAVKDVFGY EHTVPTHQGR GAEQILFPCL VARMKGDKPV
FISNYHFDTT AAHVEMTGAK AINVVTEKAF DTGTYYDWKG DFDLEKLEAT IRQHGAQNVA
GIIVTITCNS AGGQPVSMAN IREAAAIAKR HGITVIIDSA RFCENAWFIK QREAGYADKS
IREIIREMYS YGDVLTCSAK KDPIVNIGGL CCIKEDVDLF RAVQVRCVPM EGFVTYGGLA
GRDMEALAIG LYEGTDEHFL TYRIKQVEYL GERLRQGGVP IQYPTGGHAV FIDAKLMLPH
IPGNQFPAHA LANEVYIEGG VRGVEIGSLL LGRDPATGLQ KESPLELLRL AIPRRVYTND
HMDYIADTVI AVLDRASSIK GLEFTYEPPV LRHFTARLRP IA
//
