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Database: UniProt
Entry: A0A327WZ15_9GAMM
LinkDB: A0A327WZ15_9GAMM
Original site: A0A327WZ15_9GAMM 
ID   A0A327WZ15_9GAMM        Unreviewed;       347 AA.
AC   A0A327WZ15;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=L-threonine aldolase {ECO:0000313|EMBL:RAJ98990.1};
GN   ORFNames=B0I24_104194 {ECO:0000313|EMBL:RAJ98990.1};
OS   Aliidiomarina maris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Aliidiomarina.
OX   NCBI_TaxID=531312 {ECO:0000313|EMBL:RAJ98990.1, ECO:0000313|Proteomes:UP000249203};
RN   [1] {ECO:0000313|EMBL:RAJ98990.1, ECO:0000313|Proteomes:UP000249203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.15366 {ECO:0000313|EMBL:RAJ98990.1,
RC   ECO:0000313|Proteomes:UP000249203};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUN-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   -!- 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:RAJ98990.1}.
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DR   EMBL; QLMD01000004; RAJ98990.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A327WZ15; -.
DR   Proteomes; UP000249203; 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;
FT   DOMAIN          5..288
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         199
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   347 AA;  36769 MW;  FC836710DB6B3185 CRC64;
     MEVIDFRSDT LTKPTPDMRA AMASAEVGDD VYGEDPTINA LEQRVAAMLG KPAALLCTSG
     TQSNLLGILS HCQRGEEYIV GAPYHTYKYE AGGAAVLGGV VPHTVSLEAD GSVAAATLRG
     AVKADDPHFP ISRLIALENT HLGRVISQAQ MWQAREVADE FGLRLHLDGA RLANASVATG
     LSLAELAQPF DSVSLCCSKG LGAPVGSLLI GSEELIGRAR RWRKMLGGGM RQAGVIAAAI
     DYALTHHMAR LADDHTHAEG LSQQLGTRLA SLAEHVQVAP AHTNMVYLNF ADPQVAQQVS
     TAAREAGILV PASAAMRLVT HLDITSQMIE KTVDILTKVI TETVQAR
//
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