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Database: UniProt
Entry: A0A086D2Y1_9GAMM
LinkDB: A0A086D2Y1_9GAMM
Original site: A0A086D2Y1_9GAMM 
ID   A0A086D2Y1_9GAMM        Unreviewed;       351 AA.
AC   A0A086D2Y1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=L-threonine aldolase {ECO:0000256|PIRNR:PIRNR038940};
DE            EC=4.1.2.48 {ECO:0000256|PIRNR:PIRNR038940};
GN   ORFNames=GY26_11975 {ECO:0000313|EMBL:KFF48795.1};
OS   Gammaproteobacteria bacterium MFB021.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1492922 {ECO:0000313|EMBL:KFF48795.1, ECO:0000313|Proteomes:UP000028732};
RN   [1] {ECO:0000313|EMBL:KFF48795.1, ECO:0000313|Proteomes:UP000028732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MFB021 {ECO:0000313|EMBL:KFF48795.1,
RC   ECO:0000313|Proteomes:UP000028732};
RA   Joseph T.C., Baby A., Varghese A.M., Reghunathan D., Murugadas V.,
RA   Lalitha K.V.;
RT   "Draft Genome sequence of a halophilic and highly halotolerant unknown
RT   Gammaproteobacteria strain MFB021.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the cleavage of L-allo-threonine and L-threonine to
CC       glycine and acetaldehyde. {ECO:0000256|PIRNR:PIRNR038940}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-allo-threonine = acetaldehyde + glycine;
CC         Xref=Rhea:RHEA:26209, ChEBI:CHEBI:15343, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:58585; EC=4.1.2.48;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038940};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine = acetaldehyde + glycine; Xref=Rhea:RHEA:19625,
CC         ChEBI:CHEBI:15343, ChEBI:CHEBI:57305, ChEBI:CHEBI:57926; EC=4.1.2.48;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038940};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRNR:PIRNR038940};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the threonine aldolase family.
CC       {ECO:0000256|ARBA:ARBA00006966, ECO:0000256|PIRNR:PIRNR038940}.
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:KFF48795.1}.
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DR   EMBL; JNVT01000082; KFF48795.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A086D2Y1; -.
DR   STRING; 1492922.GY26_11975; -.
DR   eggNOG; COG2008; Bacteria.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000028732; Unassembled WGS sequence.
DR   GO; GO:0008732; F:L-allo-threonine aldolase activity; IEA:RHEA.
DR   GO; GO:0006567; P:threonine catabolic process; IEA:UniProtKB-UniRule.
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; IPR026273; Low_specificity_L-TA_bact.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   PANTHER; PTHR48097:SF5; LOW SPECIFICITY L-THREONINE ALDOLASE; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF038940; Low_specificity_LTA; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|PIRNR:PIRNR038940};
KW   Pyridoxal phosphate {ECO:0000256|PIRNR:PIRNR038940}.
FT   DOMAIN          10..296
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   351 AA;  38409 MW;  02BFC9C15E0A83E8 CRC64;
     MTSDCTPRFL ASDNTSGICP EALDYLIQAN ASDDLAYGND VWTHRAADRF RELFDYDCDV
     FFVFNGTAAN SLTLAALGQS YHSVICHELA HIETDECGGP EFFSNGSKLL TCPGEEGKLT
     PEGIERLVVR RSDIHYPKPR VVSITQATEV GTVYSREELL AIRTMADKYD LRVHMDGARF
     ANACSALDAT PAELTWQVGV DVLCFSGTKN GLPLGEAILF FNKGLAEDFA YRCKQAGQLA
     SKMRFIAAPW LGLLETGAWR RNADHANAMA RYLAEGLAAL PGVRPMFPTQ ANSVFVSLPA
     PVIEALRARG WTFYTFIGAG GARFVCSWNT TTELLDDLLT DARAALDHAA R
//
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