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Database: UniProt
Entry: A0A1T1I2W3_9PSED
LinkDB: A0A1T1I2W3_9PSED
Original site: A0A1T1I2W3_9PSED 
ID   A0A1T1I2W3_9PSED        Unreviewed;       334 AA.
AC   A0A1T1I2W3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Low-specificity L-threonine aldolase {ECO:0000313|EMBL:OOV96444.1};
GN   ORFNames=MF4836_14520 {ECO:0000313|EMBL:OOV96444.1};
OS   Pseudomonas sp. MF4836.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1960827 {ECO:0000313|EMBL:OOV96444.1, ECO:0000313|Proteomes:UP000190183};
RN   [1] {ECO:0000313|Proteomes:UP000190183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MF4836 {ECO:0000313|Proteomes:UP000190183};
RA   Fagerlund A.;
RT   "Genome sequencing of bacteria from food industry.";
RL   Submitted (FEB-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   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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:OOV96444.1}.
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DR   EMBL; MVOL01000005; OOV96444.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T1I2W3; -.
DR   STRING; 1960827.MF4836_14520; -.
DR   Proteomes; UP000190183; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
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; IPR023603; Low_specificity_L-TA-like.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; NF041359; GntG_guanitoxin; 1.
DR   PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF017617; Thr_aldolase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
FT   DOMAIN          5..284
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         199
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   334 AA;  35702 MW;  68A7B6E58E6403CB CRC64;
     MSVIDLRSDT VTQPSAGMLE AMAGARTGDD VYGEDPTVNQ LEADLAQRLG FAAALFVPSG
     TMSNLLGLMA HCERGDEYIV GQQAHTYKYE GGGAAVLGSI QPQPLEFQDD GSLDLAQVAA
     AIKPDDFHFA RSRLLALENT MQGKVLPLAY LAQARAFTRE HGLALHLDGA RVYNAAVKLG
     VDAREITRHF DSVSVCLSKG LGAPVGSVLC GSEQLIAKAR RLRKMVGGGM RQAGILAAAG
     LYALEHQVQR LADDHANARL LADGLREAGY SVEPVQTNMV YAQVGDRAEA LKAFAGERGI
     RLGAASRLRM VTHLDVSRAQ IEQVVDAFAE FSRN
//
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