ID   A0A0F2C7Y0_9MICO        Unreviewed;       355 AA.
AC   A0A0F2C7Y0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Low specificity L-threonine aldolase {ECO:0000313|EMBL:KJQ54004.1};
DE            EC=4.1.2.48 {ECO:0000313|EMBL:KJQ54004.1};
GN   Name=ltaE {ECO:0000313|EMBL:KJQ54004.1};
GN   ORFNames=RS85_02073 {ECO:0000313|EMBL:KJQ54004.1};
OS   Microbacterium sp. SA39.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1263625 {ECO:0000313|EMBL:KJQ54004.1, ECO:0000313|Proteomes:UP000033425};
RN   [1] {ECO:0000313|EMBL:KJQ54004.1, ECO:0000313|Proteomes:UP000033425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA39 {ECO:0000313|EMBL:KJQ54004.1,
RC   ECO:0000313|Proteomes:UP000033425};
RA   Corretto E., Antonielli L., Sessitsch A., Kidd P., Weyens N., Brader G.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (JAN-2015) 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:KJQ54004.1}.
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DR   EMBL; JXRU01000034; KJQ54004.1; -; Genomic_DNA.
DR   RefSeq; WP_046013366.1; NZ_JXRU01000034.1.
DR   AlphaFoldDB; A0A0F2C7Y0; -.
DR   STRING; 1263625.RS85_02073; -.
DR   PATRIC; fig|1263625.4.peg.2084; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000033425; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd06502; TA_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   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;
KW   Lyase {ECO:0000313|EMBL:KJQ54004.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033425}.
FT   DOMAIN          12..279
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   355 AA;  38216 MW;  D503BF49B7C99BB4 CRC64;
     MSLTHDPAIR GFASDNYSGI HPEVLAAIAA ANGGHQVAYG EDAYTVRLQE VFQAHFGEGV
     QAFPVFNGTG ANVTGLQSML PRWGAVIAAS SAHINVDEGG APEKIGGFKL LTVPTDDGKL
     TPELIDREAW GWGDEHRAQP LVVSITQSTE LGTLYSADEI RTIADHAHER GMKLHLDGAR
     LSNAAAALDL PLRAFTRDAG VDVLSFGGTK NGAMLGEAIV VLNPAASEGL AYSRKFNMQL
     SSKMRFVSAQ LIALLEGDLW LRNARHANAM AARLRSEVEA GIVDGSIRGV SFTQPTQSNG
     VFATLPDGVA DSLRESFRFY DWDAVRNEVR WMCSFDTEES DVDAFVAELS RLTRA
//