TNAA_HAES1
ID TNAA_HAES1 Reviewed; 471 AA.
AC Q0I3R5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=HS_0801;
OS Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=205914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129Pt;
RX PubMed=17172329; DOI=10.1128/jb.01422-06;
RA Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA Xie G., Inzana T.J.;
RT "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT influenzae Rd.";
RL J. Bacteriol. 189:1890-1898(2007).
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; CP000436; ABI25076.1; -; Genomic_DNA.
DR RefSeq; WP_011608954.1; NC_008309.1.
DR AlphaFoldDB; Q0I3R5; -.
DR SMR; Q0I3R5; -.
DR STRING; 205914.HS_0801; -.
DR EnsemblBacteria; ABI25076; ABI25076; HS_0801.
DR KEGG; hso:HS_0801; -.
DR eggNOG; COG3033; Bacteria.
DR HOGENOM; CLU_047223_0_0_6; -.
DR OMA; EMYQYGD; -.
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_1000017732"
FT MOD_RES 270
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00544"
SQ SEQUENCE 471 AA; 53107 MW; 515618F31CFDA8A6 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 DAMVPMGGLL CFKDNSMEDV YNECRTLCVV
QEGFPTYGGL EGGAMERLAV GLRDGMRQDW LAYRISQIEY LVQGLEKIGV VCQQPGGHAA
FVDAGKLLPH IPAEQFPAQA LACELYKVAG IRSVEIGSLL LGRDPKTGQQ LPCPAELLRL
TIPRATYTQT HMDFIIEAFK RVKENAKNIK GLDFTYEPKV LRHFTARLKE I