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Database: UniProt
Entry: A0A0Q7TND0_9MICO
LinkDB: A0A0Q7TND0_9MICO
Original site: A0A0Q7TND0_9MICO 
ID   A0A0Q7TND0_9MICO        Unreviewed;       355 AA.
AC   A0A0Q7TND0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:KQY98493.1};
GN   ORFNames=ASD19_06525 {ECO:0000313|EMBL:KQY98493.1};
OS   Microbacterium sp. Root53.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1736553 {ECO:0000313|EMBL:KQY98493.1, ECO:0000313|Proteomes:UP000051407};
RN   [1] {ECO:0000313|Proteomes:UP000051407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root53 {ECO:0000313|Proteomes:UP000051407};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY98493.1, ECO:0000313|Proteomes:UP000051407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root53 {ECO:0000313|EMBL:KQY98493.1,
RC   ECO:0000313|Proteomes:UP000051407};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQY98493.1}.
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DR   EMBL; LMFR01000022; KQY98493.1; -; Genomic_DNA.
DR   RefSeq; WP_055992050.1; NZ_LMFR01000022.1.
DR   AlphaFoldDB; A0A0Q7TND0; -.
DR   STRING; 1736553.ASD19_06525; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000051407; 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:UP000051407}.
FT   DOMAIN          12..278
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   355 AA;  37132 MW;  B11917C5EE26DEBE CRC64;
     MDALHDPDRR GFASDNYAGA HPEVIAAIAA ANGGHEVSYG DDAWTARLQE LFSELLGDGV
     EAFPVFNGTG ANVVALQSMV TRWGAVIAPA VAHVNTDEGG APEKVGGFKI VPVATPDAKL
     TPDLVEAVAG SRGVHQAVPQ VVSITQSTEL GTLYSVDEIA AIADRAHALG LTVHMDGARI
     ANAAAALDMP LRAFTRDVGV DVLSFGGTKN GAIGAEAVVV LDPHAVDGIP YLRKSAMQLA
     SKMRFVSAQL VALLEDDLWL RSGAHANAMA ARLRAGVEAG LAAGSIRGVA FTQPTQANGV
     FATLPPGVAD RLRERFRFYD WDEATGEVRW LTSWDTTEAD VDAFVAAIAA ETTRG
//
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