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Database: UniProt
Entry: A0A2S7TNU0_9FLAO
LinkDB: A0A2S7TNU0_9FLAO
Original site: A0A2S7TNU0_9FLAO 
ID   A0A2S7TNU0_9FLAO        Unreviewed;       339 AA.
AC   A0A2S7TNU0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:PQJ23498.1};
GN   ORFNames=BSU00_04820 {ECO:0000313|EMBL:PQJ23498.1};
OS   Tenacibaculum sp. SG-28.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=754426 {ECO:0000313|EMBL:PQJ23498.1, ECO:0000313|Proteomes:UP000239112};
RN   [1] {ECO:0000313|Proteomes:UP000239112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG-28 {ECO:0000313|Proteomes:UP000239112};
RA   Kumagai Y., Yoshizawa S., Kogure K.;
RT   "Trade-off between light-utilization and light-protection in marine
RT   flavobacteria.";
RL   Submitted (NOV-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}.
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:PQJ23498.1}.
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DR   EMBL; MQVY01000001; PQJ23498.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S7TNU0; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000239112; 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; 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:UP000239112}.
FT   DOMAIN          4..290
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   339 AA;  37278 MW;  14278494A47BAACD CRC64;
     MVINLISDTV TKPTEKMLQV MMNAAVGDDV FKGDPTVNAL QEKVANMFGM EDALFFPSGT
     MANQTAIKIH THPGDRMFCD KWAHVYNYEG GGAAFNSGVT SCLIDGDRGM FTASQLQKLM
     HGKSDIHAPY NRLVCVENTT NKGGGGCWDF SELEKIQKVA KANELSYHLD GARLFNALVA
     KKQSPEQYGA LFDTISICLS KGLGAPVGSV LVGSKKHIAS ALRVRKLFGG GMRQAGYLAA
     AGIYALDNHV DRLAKDHENA KIIGETLENC SFVKKVEKIE TNIVIFYVND SIKPEDFMQR
     MADKGILFIS MGEGKLRMVT HLDFTEQMLS LLCKELKEY
//
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