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Database: UniProt
Entry: A0A1G4W987_9MYCO
LinkDB: A0A1G4W987_9MYCO
Original site: A0A1G4W987_9MYCO 
ID   A0A1G4W987_9MYCO        Unreviewed;       360 AA.
AC   A0A1G4W987;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=L-threonine aldolase {ECO:0000313|EMBL:SCX18844.1};
GN   ORFNames=SAMN02799620_02568 {ECO:0000313|EMBL:SCX18844.1};
OS   Mycolicibacterium fluoranthenivorans.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=258505 {ECO:0000313|EMBL:SCX18844.1, ECO:0000313|Proteomes:UP000199707};
RN   [1] {ECO:0000313|Proteomes:UP000199707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UNC267MFSha1.1M11 {ECO:0000313|Proteomes:UP000199707};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FMUB01000005; SCX18844.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4W987; -.
DR   STRING; 1502745.SAMN02799620_02568; -.
DR   Proteomes; UP000199707; 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          14..282
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   360 AA;  38568 MW;  AAE8C76D56389E6B CRC64;
     MPVTRLHDPS WRGFASDNYA GVHPEVLEAI AVANGGHQVA YGGDVYTARL QEVIREHFGA
     QAEVFPIFNG TGANVVALTS VLPRWGAVVT ASTAHINTDE AGAPERMTGI KLLTVPTADG
     KLDPELAARE AWGWGDEHRA QPLAVSITQA TEMGTVYTVD EVRALTDFAH ARGMTVHMDG
     SRLWNAAAAL DVPLRAFTTD AGIDIVSLGG TKNGLLGAEA VVVLNPDRAV GLVYLRKLTM
     QLASKMRFAS AQLLALFDGG LGIRSAGHAN AMAARLRAAL AAGVAEGTLP GLAFTQQTSA
     NAVFATLPIA IADRIRERVR FYDWDRARGE VRWMAAWDTT EADVDHFVTV IEEEFARESL
//
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