ID A0A3A9UT63_9FLAO Unreviewed; 341 AA.
AC A0A3A9UT63;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:AXT19917.1};
GN ORFNames=D1817_08475 {ECO:0000313|EMBL:AXT19917.1};
OS Flavobacteriaceae bacterium.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1871037 {ECO:0000313|EMBL:AXT19917.1, ECO:0000313|Proteomes:UP000260281};
RN [1] {ECO:0000313|EMBL:AXT19917.1, ECO:0000313|Proteomes:UP000260281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU392 {ECO:0000313|EMBL:AXT19917.1,
RC ECO:0000313|Proteomes:UP000260281};
RA Song W., Thomas T., Edwards R.;
RT "Complete genome sequences of pooled genomic DNA from 10 marine bacteria
RT using PacBio sequencing.";
RL Submitted (AUG-2018) 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; CP031964; AXT19917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9UT63; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000260281; Chromosome.
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:UP000260281}.
FT DOMAIN 4..289
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 201
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 341 AA; 37561 MW; 2CD12EB0E20FB2E1 CRC64;
MIIDLRSDTV TKPTQGMLDA MMSASVGDDV YKEDPTVNAL EEKVAEMFGK PKALFFPTGT
MANQAAINLH TRPGEQVICD KYAHIYNYEG GGASFNSGVS CRLIDGDRGM YTVEQAAAAI
NPPDFYHSPL TSLIEIENTT NKGGGACWDF NEIKKLQKLS KDNGLGFHLD GARLWNALIA
TEETPKQYGE AFDTISVCLS KGLGCPIGSV LTGDAEFMDN AIRIRKILGG GMRQVGYLAA
AGIYALDHQF ERLQEDHNKA KELESVLGTL SFIKKVEPVE TNIIIFELND TVDEVKFMSE
LKTNNIHIIG MGGGKLRMVT HLDYTDTMHQ FLLEKLKGFQ F
//
