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Database: UniProt
Entry: F4L6A6_HALH1
LinkDB: F4L6A6_HALH1
Original site: F4L6A6_HALH1 
ID   F4L6A6_HALH1            Unreviewed;       455 AA.
AC   F4L6A6;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
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=Halhy_0884 {ECO:0000313|EMBL:AEE48788.1};
OS   Haliscomenobacter hydrossis (strain ATCC 27775 / DSM 1100 / LMG 10767 / O).
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Haliscomenobacteraceae;
OC   Haliscomenobacter.
OX   NCBI_TaxID=760192 {ECO:0000313|EMBL:AEE48788.1, ECO:0000313|Proteomes:UP000008461};
RN   [1] {ECO:0000313|EMBL:AEE48788.1, ECO:0000313|Proteomes:UP000008461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27775 / DSM 1100 / LMG 10767 / O
RC   {ECO:0000313|Proteomes:UP000008461};
RX   PubMed=21886862; DOI=10.4056/sigs.1964579;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Daligault H., Lapidus A., Zeytun A., Nolan M., Lucas S., Del Rio T.G.,
RA   Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M.,
RA   Verbarg S., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of Haliscomenobacter hydrossis type strain (O).";
RL   Stand. Genomic Sci. 4:352-360(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 1100;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Pagani I.,
RA   Daligault H., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Verbarg S., Frueling A.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "Complete sequence of chromosome of Haliscomenobacter hydrossis DSM 1100.";
RL   Submitted (APR-2011) 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: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; CP002691; AEE48788.1; -; Genomic_DNA.
DR   RefSeq; WP_013763348.1; NC_015510.1.
DR   AlphaFoldDB; F4L6A6; -.
DR   SMR; F4L6A6; -.
DR   STRING; 760192.Halhy_0884; -.
DR   GeneID; 78190868; -.
DR   KEGG; hhy:Halhy_0884; -.
DR   eggNOG; COG3033; Bacteria.
DR   HOGENOM; CLU_047223_0_0_10; -.
DR   OrthoDB; 9764079at2; -.
DR   UniPathway; UPA00332; UER00452.
DR   Proteomes; UP000008461; 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:AEE48788.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00544}; Reference proteome {ECO:0000313|Proteomes:UP000008461};
KW   Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079, ECO:0000256|HAMAP-
KW   Rule:MF_00544}.
FT   DOMAIN          46..419
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         256
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00544,
FT                   ECO:0000256|PIRSR:PIRSR611166-50"
SQ   SEQUENCE   455 AA;  50643 MW;  C9D9E46668548BFD CRC64;
     MKTIIEPFRI KSVEPIRMTS REERKLLMRA AHYNPFLLHS DDVMIDFLTD SGTSAMSAAQ
     WAGIMRGDES YAGSPSFGRF EAAVRELMPF EHIIPTHQGR AAEKILFSIV GGKGKIIPNN
     AHFDTTRANV EYSGATALDL LIVEGRNPSS LHPFKGNMDV QKLRTLLEAE HQSVPLVMLT
     LTNNSGGGQP VSMENIKAVK ALCQEFGKPL FFDSCRFAEN AYFIKLREPD YQHHSVKSIV
     REMFSYADGM TMSAKKDALV NIGGWLALNN ADWAQQARNL LIITEGFPTY GGLAGRDLEA
     IAVGLSEIVE EDYLQYRIRS TQYLGEALLK LGIPIVQPVG GHAVYIDAKA FLPHIPALQY
     PAQALVVAMY EIGGIRACEI GSVMFGRQTD GSEKAAAMEL VRLAIPRRVY TQSHIDYVIE
     CFETIVAEKD QLRGMKIVEE PPTLRHFTAK FDWVD
//
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