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Database: UniProt
Entry: A0A074LKI4_9BACT
LinkDB: A0A074LKI4_9BACT
Original site: A0A074LKI4_9BACT 
ID   A0A074LKI4_9BACT        Unreviewed;       337 AA.
AC   A0A074LKI4;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:KEO74352.1};
GN   ORFNames=EL17_06345 {ECO:0000313|EMBL:KEO74352.1};
OS   Anditalea andensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Anditalea.
OX   NCBI_TaxID=1048983 {ECO:0000313|EMBL:KEO74352.1, ECO:0000313|Proteomes:UP000027821};
RN   [1] {ECO:0000313|EMBL:KEO74352.1, ECO:0000313|Proteomes:UP000027821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LY1 {ECO:0000313|EMBL:KEO74352.1,
RC   ECO:0000313|Proteomes:UP000027821};
RA   Yang L., Wei S., Tay Q.X.M.;
RT   "Characterization and application of a salt tolerant electro-active
RT   bacterium.";
RL   Submitted (APR-2014) 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:KEO74352.1}.
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DR   EMBL; JMIH01000015; KEO74352.1; -; Genomic_DNA.
DR   RefSeq; WP_035072271.1; NZ_JMIH01000015.1.
DR   AlphaFoldDB; A0A074LKI4; -.
DR   STRING; 1048983.EL17_06345; -.
DR   eggNOG; COG2008; Bacteria.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000027821; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000027821}.
FT   DOMAIN          4..289
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         200
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   337 AA;  37008 MW;  C4E049582A84CA77 CRC64;
     MIIELRSDTF TRPTPAMQEA MFSASVGDDV FGEDPTVNAL EQKLADMFGM ETGLYCPSGT
     MTNQIAIRLH TGPQTEIICH KYSHIYLYEG GGIMSNSMAS VKLLDGPLGK ISPADILENI
     NPDDVHAPET TLVALENTMN KGGGSIYTLE EIKPIKDICV NHGLRLHLDG ARLFNALTVT
     GENPKDWGQA FDTISICLSK GLGCPVGSVL LGNKAFIKKA RKVRKALGGG MRQAGILAAA
     GIYALDHHVE RLAEDHRKAK KIGEILEKQS WVLEVFPVQT NIVIVKLKDA TPAEMLAKLA
     EKEIRAVKFG KDQIRFVTHL DFTDEHLDEF ENRVNEI
//
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