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Database: UniProt
Entry: X7E775_9GAMM
LinkDB: X7E775_9GAMM
Original site: X7E775_9GAMM 
ID   X7E775_9GAMM            Unreviewed;       346 AA.
AC   X7E775;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=L-threonine aldolase {ECO:0000256|PIRNR:PIRNR038940};
DE            EC=4.1.2.48 {ECO:0000256|PIRNR:PIRNR038940};
GN   ORFNames=MUS1_08080 {ECO:0000313|EMBL:ETX11889.1};
OS   Marinomonas ushuaiensis DSM 15871.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=1122207 {ECO:0000313|EMBL:ETX11889.1, ECO:0000313|Proteomes:UP000054058};
RN   [1] {ECO:0000313|EMBL:ETX11889.1, ECO:0000313|Proteomes:UP000054058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15871 {ECO:0000313|EMBL:ETX11889.1,
RC   ECO:0000313|Proteomes:UP000054058};
RA   Lai Q., Shao Z.S.;
RT   "Marinomonas ushuaiensis DSM 15871 Genome Sequencing.";
RL   Submitted (JAN-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:ETX11889.1}.
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DR   EMBL; JAMB01000002; ETX11889.1; -; Genomic_DNA.
DR   RefSeq; WP_036159595.1; NZ_JAMB01000002.1.
DR   AlphaFoldDB; X7E775; -.
DR   STRING; 1122207.MUS1_08080; -.
DR   PATRIC; fig|1122207.3.peg.931; -.
DR   eggNOG; COG2008; Bacteria.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000054058; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054058}.
FT   DOMAIN          5..291
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   346 AA;  37254 MW;  C39B481D164C083E CRC64;
     MKVTFASDNT AGASESVFQA MMDAAQGDAM PYGNDEVTAE VTEMLSALFE CDLDVFMVST
     GTAANVLSLG AMTPSWGSVL CHSESHILND ECSAPEFYTG GARLIGIDGQ DAKIDPIKLK
     ALTYHKIGDV HSCQPSAVSL SQVTEVGSVY SLEELRAITD IAKEAGLPVH MDGARFANAL
     VALGCTPAEM TWKAGIDILS FGATKNGTMA AEAIVVFNKS LSKDLAFRRK RGGHLHSKMR
     LLSSQMKAYL TDDLWRKNAE QANSMMALLQ DGLATIPGVK INTPAQANMV FCTFPKGMTE
     HLTEQDFTFY GGRWGEGVVR LVTSFRTPKE GVEAFIHSAK AFVEKT
//
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