ID   A0A2M8WJ78_9MICO        Unreviewed;       365 AA.
AC   A0A2M8WJ78;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=L-threonine aldolase {ECO:0000313|EMBL:PJI90948.1};
GN   ORFNames=CLV34_2206 {ECO:0000313|EMBL:PJI90948.1};
OS   Luteimicrobium subarcticum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Luteimicrobium.
OX   NCBI_TaxID=620910 {ECO:0000313|EMBL:PJI90948.1, ECO:0000313|Proteomes:UP000231586};
RN   [1] {ECO:0000313|EMBL:PJI90948.1, ECO:0000313|Proteomes:UP000231586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22413 {ECO:0000313|EMBL:PJI90948.1,
RC   ECO:0000313|Proteomes:UP000231586};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): From Individual Species to Whole Genera.";
RL   Submitted (NOV-2017) 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:PJI90948.1}.
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DR   EMBL; PGTZ01000009; PJI90948.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M8WJ78; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000231586; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000231586}.
FT   DOMAIN          26..312
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   365 AA;  38481 MW;  B96940BD713CE0F0 CRC64;
     MTTPSPLPDP TPRTAAAPSP LASRSFASDN YAGAHPEVLA ALVAANDGHA VSYGDDPWTD
     RLQDVVRGHF GPRATAYPVF NGTGANVVAL ATALPRWGAV VTPSTAHVAV DENGAPERVG
     GLKLLTVDTP DGRLTPELLD REAWGWGDAH RAQPLGVSVS QSTELGTTYT VDALRELVEH
     AHRLGMVVHV DGARLSNAAA HLGVGLGELT TDLGVDVVSL GGTKNGLVLG EAVVVLNPDV
     GDGIEYVRKM TMQLGSKLRF VSAQLVALYG SDLWRTSAAH ANAMATRLRA GLAGVEGVVP
     TRPTESNAVF AALAPDAADR VRERFRFYDW DARRDDGLVE VRWMCAWDTT EADVDAFVDA
     VAGAV
//