TNAA_HISS2
ID TNAA_HISS2 Reviewed; 471 AA.
AC B0UTZ3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=HSM_1270;
OS Histophilus somni (strain 2336) (Haemophilus somnus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=228400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2336;
RG US DOE Joint Genome Institute;
RA Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA Dyer D.W., Inzana T.J.;
RT "Complete sequence of Haemophilus somnus 2336.";
RL Submitted (FEB-2008) 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: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; CP000947; ACA30999.1; -; Genomic_DNA.
DR RefSeq; WP_012340430.1; NC_010519.1.
DR AlphaFoldDB; B0UTZ3; -.
DR SMR; B0UTZ3; -.
DR STRING; 228400.HSM_1270; -.
DR EnsemblBacteria; ACA30999; ACA30999; HSM_1270.
DR KEGG; hsm:HSM_1270; -.
DR HOGENOM; CLU_047223_0_0_6; -.
DR OMA; EMYQYGD; -.
DR OrthoDB; 91973at2; -.
DR UniPathway; UPA00332; UER00452.
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 TIGRFAMs; TIGR02617; tnaA_trp_ase; 1.
DR PROSITE; PS00853; BETA_ELIM_LYASE; 1.
PE 3: Inferred from homology;
KW Lyase; Pyridoxal phosphate; Tryptophan catabolism.
FT CHAIN 1..471
FT /note="Tryptophanase"
FT /id="PRO_1000081942"
FT MOD_RES 270
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00544"
SQ SEQUENCE 471 AA; 53061 MW; D2521DE4CE3E7A81 CRC64;
MENFKHLPEP FRIRVIEPVK RTTRAYRDEA ILKAGMNLFL LDSEDIFIDL LTDSGTGAVT
QDMQAAMLRG DEAYSGSRSY YALANAVKEI FGYEYTIPTH QGRGAEQIYI PVLIKKREQE
KGLDRNKMVV FSNYFFDTTQ GHSQLNGATV RNVYIKEAFD TDVDHDFKGN FDLEKLEQGI
LEVGANNVPY IVCTITCNSA GGQPVSLANM KAMYQIARKY DIPVIMDSAR FAENAYFIQQ
REAEYKDWTI EQITYESYKY ADALAMSAKK DAMVPIGGLL CFKDNSMEDV YNECRTLCVV
QEGFPTYGGL EGGAMERLAV GLRDGMRQDW LAYRISQIEY LVQGLEKIGV VCQQPGGHAA
FVDAGKLLPH IPAEQFPAQA LACELYKVAG IRSVEIGSLL LGRDPKTGQQ LPCPAELLRL
TIPRATYTQT HMDFIIEAFK QVKENAKNIK GLDFTYEPKV LRHFTARLKE I