TNAA2_SYMTH
ID TNAA2_SYMTH Reviewed; 454 AA.
AC P31015; Q67SB9; Q9R5M8;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Tryptophanase 2;
DE EC=4.1.99.1;
DE AltName: Full=L-tryptophan indole-lyase 2;
DE Short=TNase 2;
GN Name=tnaA2; Synonyms=tna-2; OrderedLocusNames=STH439;
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-35.
RC STRAIN=IAM 13621;
RX PubMed=1339259; DOI=10.1128/aem.58.8.2633-2642.1992;
RA Hirahara T., Suzuki S., Horinouchi S., Beppu T.;
RT "Cloning, nucleotide sequences, and overexpression in Escherichia coli of
RT tandem copies of a tryptophanase gene in an obligately symbiotic
RT thermophile, Symbiobacterium thermophilum.";
RL Appl. Environ. Microbiol. 58:2633-2642(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863;
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2-36.
RC STRAIN=T / IAM 14863;
RX PubMed=1368766; DOI=10.1271/bbb1961.55.3059;
RA Suzuki S., Hirahara T., Horinouchi S., Beppu T.;
RT "Purification and properties of thermostable tryptophanase from an
RT obligately symbiotic thermophile, Symbiobacterium thermophilum.";
RL Agric. Biol. Chem. 55:3059-3066(1991).
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via pyruvate
CC pathway; indole and pyruvate from L-tryptophan: step 1/1.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC {ECO:0000305}.
CC -!- CAUTION: Tna2 is expressed in strain T but expression in strain IAM
CC 13621 has not been proven. {ECO:0000305}.
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DR EMBL; AB010832; BAA24687.1; -; Genomic_DNA.
DR EMBL; AP006840; BAD39424.1; -; Genomic_DNA.
DR PIR; B49022; B49022.
DR RefSeq; WP_011194573.1; NC_006177.1.
DR AlphaFoldDB; P31015; -.
DR SMR; P31015; -.
DR STRING; 292459.STH439; -.
DR EnsemblBacteria; BAD39424; BAD39424; STH439.
DR KEGG; sth:STH439; -.
DR eggNOG; COG3033; Bacteria.
DR HOGENOM; CLU_047223_0_0_9; -.
DR OMA; MFPHIPY; -.
DR OrthoDB; 91973at2; -.
DR BRENDA; 4.1.99.1; 6177.
DR UniPathway; UPA00332; UER00452.
DR Proteomes; UP000000417; Chromosome.
DR GO; GO:0009034; F:tryptophanase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF01212; Beta_elim_lyase; 1.
DR PIRSF; PIRSF001386; Trpase; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00853; BETA_ELIM_LYASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome;
KW Tryptophan catabolism.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1339259,
FT ECO:0000269|PubMed:1368766"
FT CHAIN 2..454
FT /note="Tryptophanase 2"
FT /id="PRO_0000195623"
FT MOD_RES 255
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 135
FT /note="Missing (in Ref. 1; BAA24687)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 454 AA; 50661 MW; 5EB609F6EFE866CB CRC64;
MPKGEPFKIK MVEPIRLIPR EDREAAIKAA HYNPFLLRSS DVYIDLLTDS GTGAMSQFQW
SAMMLGDESY AGASSYYRLK EAVTDITGYE YVLPTHQGRG AEKSAFAQLI TRPGMYVLSN
MFFDTTRGHV QLAGGRPIDL LLDVPTEEYH PFKGNMDTAR LEAFIQEHGA ENIACIVMTV
TNNSAGGQPV SMANIRETSR IARKYGILLL FDVARYAENC HFIRMREEGY ADKAPIDIAR
EMFSYGDGLM MSAKKDALVN IGGLLAFKDE ELYTRVGGTV VPFEGFLTYG GLAGRDLEAM
AVGLREALDP DYLAYRVGQV EYLGNLLRSA GIPIQWPVGG HAVFIDAAKF LPHIPWDQFP
GHALTVALYQ EGGVRTVEVG SLVMGRDPET GENVRSPFEF TRLAIPRRVY TNLHLEDVAE
TVINAFQKRE QIRGVKFTRE PKVLRHFTAH FDLV
