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Database: UniProt
Entry: A0A1X1MQQ0_9VIBR
LinkDB: A0A1X1MQQ0_9VIBR
Original site: A0A1X1MQQ0_9VIBR 
ID   A0A1X1MQQ0_9VIBR        Unreviewed;       354 AA.
AC   A0A1X1MQQ0;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:ORT49594.1};
GN   ORFNames=ST37_14560 {ECO:0000313|EMBL:ORT49594.1};
OS   Vibrio sp. qd031.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1603038 {ECO:0000313|EMBL:ORT49594.1, ECO:0000313|Proteomes:UP000193432};
RN   [1] {ECO:0000313|EMBL:ORT49594.1, ECO:0000313|Proteomes:UP000193432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=qd031 {ECO:0000313|Proteomes:UP000193432};
RA   Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ORT49594.1, ECO:0000313|Proteomes:UP000193432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=qd031 {ECO:0000313|Proteomes:UP000193432};
RA   Chen G.;
RT   "Denovo assembling a bacteria genome.";
RL   Submitted (MAY-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:ORT49594.1}.
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DR   EMBL; JXQD01000025; ORT49594.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1MQQ0; -.
DR   STRING; 1603038.ST37_14560; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000193432; 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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000193432}.
FT   DOMAIN          33..292
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   354 AA;  40183 MW;  D493DB9DA6169104 CRC64;
     MSQQFKNQCS IHIPGNAEPT PAEHFQLMAT WCEKHNVDHD VYGDGATLQQ FESKIATLLG
     YEAAMFVVSG TMTQPTLLEM VTQQSGKSNV VMHSSSHILL HENQGFQLQN RFNVLPVGHR
     FSPWTTNDLE QIVDPIAAVL YELPMREIGG QLPEWEELQE IKAHCRRNNI HMHMDGARLW
     ECSAFYDKSY KEICSGFDTT YVSLYKGIGG MGGSMLCGSQ SMINAAKVWM QRVGGNLYHR
     TPYVVSAMMQ FDQRIDAMPA LFKRTQELYQ LLSHYPTLQP VPIRPNSNML HLYLPHSYES
     AVNIRDTLAK EHGVWIGNPQ RTDNPMQSKI EWYVGDNLLA VSNTNLDKVF LALS
//
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