TNAA_CITK8
ID TNAA_CITK8 Reviewed; 462 AA.
AC A8AKE2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=CKO_02849;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) 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; CP000822; ABV13955.1; -; Genomic_DNA.
DR RefSeq; WP_012133668.1; NC_009792.1.
DR AlphaFoldDB; A8AKE2; -.
DR SMR; A8AKE2; -.
DR STRING; 290338.CKO_02849; -.
DR EnsemblBacteria; ABV13955; ABV13955; CKO_02849.
DR GeneID; 45136682; -.
DR KEGG; cko:CKO_02849; -.
DR HOGENOM; CLU_047223_0_0_6; -.
DR OMA; EMYQYGD; -.
DR OrthoDB; 91973at2; -.
DR UniPathway; UPA00332; UER00452.
DR Proteomes; UP000008148; 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 TIGRFAMs; TIGR02617; tnaA_trp_ase; 1.
DR PROSITE; PS00853; BETA_ELIM_LYASE; 1.
PE 3: Inferred from homology;
KW Lyase; Pyridoxal phosphate; Reference proteome; Tryptophan catabolism.
FT CHAIN 1..462
FT /note="Tryptophanase"
FT /id="PRO_1000017729"
FT MOD_RES 261
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00544"
SQ SEQUENCE 462 AA; 51941 MW; 391082CD944E7A01 CRC64;
MKRIPEPFRI KMVENIRMTT WDDRVKALEE AGYNPFLLRS DDVYIDLLTD SGTGAMSDRQ
WSGLMMGDEA YAGSRNYYHL CDKVKELIGY PFTIPTHQGR GAEQILFPCL IARRNAEKPV
FISNFHFDTT AAHVELNGAK AINVVTPKAF DTTSWYDWKG NFDIDLLNAT IAEHGAENVA
AIITTVTCNS SGGQPVSIAN MREVYQIAKR HNIPVVIDSA RFCENAWFIK QREEGYADKT
VKEIVREMYQ YGDMLTMSAK KDPMVNIGGL CCFRDDEDLF NDVRIRCVPM EGFVTYGGLA
GRDMEALAIG LEEGMNEDFL AYRINQVEYL GERLREGGIP IQYPTGGHAV FVDAKLLLPH
IPAEQFPAHA LNNELYLEAG IRSVEIGSLL LGRDPATGKQ KPSPMELLRL TIPRRVYTND
HMDYIADALI AVKARAASIK GLTFTYEPPV LRHFVARLKP VK