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Database: UniProt
Entry: M2BUP5_TREDN
LinkDB: M2BUP5_TREDN
Original site: M2BUP5_TREDN 
ID   M2BUP5_TREDN            Unreviewed;       351 AA.
AC   M2BUP5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein {ECO:0000259|Pfam:PF01212};
GN   ORFNames=HMPREF9733_00916 {ECO:0000313|EMBL:EMB25784.1};
OS   Treponema denticola SP33.
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=999437 {ECO:0000313|EMBL:EMB25784.1, ECO:0000313|Proteomes:UP000016183};
RN   [1] {ECO:0000313|EMBL:EMB25784.1, ECO:0000313|Proteomes:UP000016183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP33 {ECO:0000313|EMBL:EMB25784.1,
RC   ECO:0000313|Proteomes:UP000016183};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Blanton J.M., Fenno C.J.,
RA   Baranova O.V., Mathney J., Dewhirst F.E., Izard J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Treponema denticola SP33.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the threonine aldolase family.
CC       {ECO:0000256|ARBA:ARBA00006966}.
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:EMB25784.1}.
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DR   EMBL; AGDZ01000018; EMB25784.1; -; Genomic_DNA.
DR   RefSeq; WP_010694508.1; NZ_KB442453.1.
DR   AlphaFoldDB; M2BUP5; -.
DR   PATRIC; fig|999437.3.peg.927; -.
DR   HOGENOM; CLU_049619_1_0_12; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000016183; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   PANTHER; PTHR48097:SF5; LOW SPECIFICITY L-THREONINE ALDOLASE; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
FT   DOMAIN          54..240
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   351 AA;  39295 MW;  8E9867E77DB18033 CRC64;
     MYFFINDYSE GCHPKILQTL TETNEEQTVG YGCDKYCAEA ADLILKELDA PQSKVYFFSG
     GTQTNLTMIA SVLRPHQGVI AADTGHINVH ESGAIEACGH KVLTIESANG KITAEQAEAL
     IRAHYDDPTA EHMVQPGMIY ISNPTELGTI YSKKELQALK LTAQKYSVPL YVDGARLGTA
     LTADNNDLSL ADMARYTDAF YIGGTKMGAL FGEALIINNQ ELQKDFRYIQ KQKGGLFAKG
     RLLGLQFKTL FTDKLYFEIG RTMNETAKLI RKGFSDRGFS FFMESETNQS FPIIENGLLA
     KIEKEFKCEF WAKITENLTA VRFCTSWATT KEAIKKLFEY VDEIKSNESK K
//
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