ID A0A135I9Y5_9GAMM Unreviewed; 336 AA.
AC A0A135I9Y5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:KXF82261.1};
GN ORFNames=ATN88_24195 {ECO:0000313|EMBL:KXF82261.1};
OS Enterovibrio coralii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Enterovibrio.
OX NCBI_TaxID=294935 {ECO:0000313|EMBL:KXF82261.1, ECO:0000313|Proteomes:UP000070529};
RN [1] {ECO:0000313|EMBL:KXF82261.1, ECO:0000313|Proteomes:UP000070529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 912 {ECO:0000313|EMBL:KXF82261.1,
RC ECO:0000313|Proteomes:UP000070529};
RA Gomez-Gil B., Enciso-Ibarra J.;
RT "Genomic Taxonomy of the Vibrionaceae.";
RL Submitted (NOV-2015) 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:KXF82261.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNTY01000026; KXF82261.1; -; Genomic_DNA.
DR RefSeq; WP_067414227.1; NZ_LNTY01000026.1.
DR AlphaFoldDB; A0A135I9Y5; -.
DR STRING; 294935.ATN88_24195; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000070529; 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:UP000070529}.
FT DOMAIN 3..285
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 336 AA; 36681 MW; A3FDD4031729A3B0 CRC64;
MIDFRSDTVT QPDQRMREAM ANAPVGDDVY GDDPTVNELE KWAAERHGFE AAVFTASGTQ
ANLLGILAHC DRGDEYLCGQ QAHNYKYEAG GAAVLGSVQP QPIENNKDGT LCFEKLAAAV
KPDDVHFART TLLSLENTIG GKVLPLDYLA KAREFVNQHN LKLHLDGARV YNASVALNVD
ITEISKHFDS MTICLSKGLG APIGSLLLGD AEYIQRARRL RKMVGGGMRQ AGILAAAGMM
ALTENVERLK DDHDNARYLS ENLGAIPGFN TFIYPVQTNI VYADIAQHID IHAIAKVLKE
QGILVSPSHK AMRFVTHKDV TKADIDALLS AIEQQL
//
