ID F2NKC8_MARHT Unreviewed; 456 AA.
AC F2NKC8;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Tryptophanase {ECO:0000256|HAMAP-Rule:MF_00544};
DE EC=4.1.99.1 {ECO:0000256|HAMAP-Rule:MF_00544};
DE AltName: Full=L-tryptophan indole-lyase {ECO:0000256|HAMAP-Rule:MF_00544};
DE Short=TNase {ECO:0000256|HAMAP-Rule:MF_00544};
GN Name=tnaA {ECO:0000256|HAMAP-Rule:MF_00544};
GN OrderedLocusNames=Marky_1642 {ECO:0000313|EMBL:AEB12377.1};
OS Marinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Marinithermus.
OX NCBI_TaxID=869210 {ECO:0000313|EMBL:AEB12377.1, ECO:0000313|Proteomes:UP000007030};
RN [1] {ECO:0000313|EMBL:AEB12377.1, ECO:0000313|Proteomes:UP000007030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14884 / JCM 11576 / T1 {ECO:0000313|Proteomes:UP000007030};
RX PubMed=22675595; DOI=10.4056/sigs.2435521;
RA Copeland A., Gu W., Yasawong M., Lapidus A., Lucas S., Deshpande S.,
RA Pagani I., Tapia R., Cheng J.F., Goodwin L.A., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Pan C., Brambilla E.M., Rohde M., Tindall B.J., Sikorski J.,
RA Goker M., Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the aerobic, heterotroph Marinithermus
RT hydrothermalis type strain (T1(T)) from a deep-sea hydrothermal vent
RT chimney.";
RL Stand. Genomic Sci. 6:21-30(2012).
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:0000256|ARBA:ARBA00001826, ECO:0000256|HAMAP-
CC Rule:MF_00544};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00544, ECO:0000256|PIRSR:PIRSR611166-50};
CC -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via pyruvate
CC pathway; indole and pyruvate from L-tryptophan: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004662, ECO:0000256|HAMAP-Rule:MF_00544}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00544}.
CC -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC {ECO:0000256|ARBA:ARBA00009721, ECO:0000256|HAMAP-Rule:MF_00544}.
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DR EMBL; CP002630; AEB12377.1; -; Genomic_DNA.
DR RefSeq; WP_013704424.1; NC_015387.1.
DR AlphaFoldDB; F2NKC8; -.
DR SMR; F2NKC8; -.
DR STRING; 869210.Marky_1642; -.
DR KEGG; mhd:Marky_1642; -.
DR eggNOG; COG3033; Bacteria.
DR HOGENOM; CLU_047223_0_0_0; -.
DR OrthoDB; 9764079at2; -.
DR UniPathway; UPA00332; UER00452.
DR Proteomes; UP000007030; 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 InterPro; IPR018176; Tryptophanase_CS.
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.
DR PROSITE; PS00853; BETA_ELIM_LYASE; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00544, ECO:0000313|EMBL:AEB12377.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00544}; Reference proteome {ECO:0000313|Proteomes:UP000007030};
KW Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079, ECO:0000256|HAMAP-
KW Rule:MF_00544}.
FT DOMAIN 46..422
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 257
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00544,
FT ECO:0000256|PIRSR:PIRSR611166-50"
SQ SEQUENCE 456 AA; 51424 MW; 34DC4E3D128C938C CRC64;
MNTIIEPFKI KMVEPIKLTT RAERERYIQE AGYNLFLLRA EDVIIDLLTD SGTSAMSAAQ
WSALMRGDES YAGARSWYRF EATVREIFGF EHVIPTHQGR AAERILFSVM VKPGMVVPNN
THFDTTRANI EYLGGRAVDL PCPEAKDPAL EAPFKGNMDT QALEALIEEV GPERIPLIMI
TVTNNSGGGQ PVSMANIREV SRIARKHGIP FYIDACRFAE NAYFIKLREE GYQNKSVREI
VAEMFSYADG CTMSAKKDAF ANIGGFLCTN DASLAQQERD LLILTEGFPT YGGLAGRDLE
AIAVGLREVL EEDYLRYRLV STRYVADHLT ERGIPVVRPA GGHAVYLDAR RFLPHLDPLE
YPGQALAVEL YLEAGIRGVE IGTVMFGKDP HTGEERPAQW DLVRLAIPRR AYTQSHMDYV
VEAVERVWAR REEIRGYRIV EEPPFLRHFT ARFEPL
//
