ID   M0HYM4_9EURY            Unreviewed;       448 AA.
AC   M0HYM4;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Tryptophanase/L-cysteine desulfhydrase, PLP-dependent {ECO:0000313|EMBL:ELZ89700.1};
DE            EC=4.1.99.1 {ECO:0000313|EMBL:ELZ89700.1};
GN   Name=tnaA {ECO:0000313|EMBL:ELZ89700.1};
GN   ORFNames=C441_15040 {ECO:0000313|EMBL:ELZ89700.1};
OS   Haloferax sulfurifontis ATCC BAA-897.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=662480 {ECO:0000313|EMBL:ELZ89700.1, ECO:0000313|Proteomes:UP000011508};
RN   [1] {ECO:0000313|EMBL:ELZ89700.1, ECO:0000313|Proteomes:UP000011508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-897 {ECO:0000313|EMBL:ELZ89700.1,
RC   ECO:0000313|Proteomes:UP000011508};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC       {ECO:0000256|ARBA:ARBA00009721}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELZ89700.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AOLM01000025; ELZ89700.1; -; Genomic_DNA.
DR   RefSeq; WP_007275790.1; NZ_AOLM01000025.1.
DR   AlphaFoldDB; M0HYM4; -.
DR   PATRIC; fig|662480.6.peg.2996; -.
DR   OrthoDB; 287201at2157; -.
DR   Proteomes; UP000011508; Unassembled WGS sequence.
DR   GO; GO:0009034; F:tryptophanase activity; IEA:UniProtKB-EC.
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   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   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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:ELZ89700.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          42..410
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   448 AA;  48579 MW;  B8A168DABB705EBA CRC64;
     MKSYKAKMVE PIELPSREER EAALERAGYN AFNLDARDVY IDLLTDSGTG TMSAEQWAAM
     IRGDEAYAGS ESFARLADSV RDVMGFEHVV PTHQGRGAEN VLYGVLLEDG DVVPNNSHFD
     TTRAHVVNQG AEPVDCPSPA SRDPNSTETF KGNFDIDAGY ALVEEVGADA IPVVVLTITN
     NSVAGQPVSM ANIRATAEFA RDIDAMFVID ACRFAENAHF IKTNEAGYEN HSVAEIARAQ
     FEHADAITMS GKKDALVNIG GFAAMRDETV FEHAKQRAIL YEGFPTYGGL SGRDIEAMAV
     GLREAVTPPY VTDRVEQVAE LGDLLVEAGV PVYQPTGGHA VYLDAGEVFP HVPKDEYPGQ
     QLVCALYLEG GVRGVELGGF AFPGTDRPDL VRLALPRRTY SREHLEHVAE TAAKVMASAG
     EYGGLEIVEE PPMKELRHFS ARLEPVSN
//