ID J3G4U9_9PSED Unreviewed; 355 AA.
AC J3G4U9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=L-threonine aldolase {ECO:0000256|PIRNR:PIRNR038940};
DE EC=4.1.2.48 {ECO:0000256|PIRNR:PIRNR038940};
GN ORFNames=PMI28_03944 {ECO:0000313|EMBL:EJM54145.1};
OS Pseudomonas sp. GM48.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144330 {ECO:0000313|EMBL:EJM54145.1, ECO:0000313|Proteomes:UP000007293};
RN [1] {ECO:0000313|EMBL:EJM54145.1, ECO:0000313|Proteomes:UP000007293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM48 {ECO:0000313|EMBL:EJM54145.1,
RC ECO:0000313|Proteomes:UP000007293};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJM54145.1}.
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DR EMBL; AKJM01000110; EJM54145.1; -; Genomic_DNA.
DR AlphaFoldDB; J3G4U9; -.
DR PATRIC; fig|1144330.3.peg.3851; -.
DR Proteomes; UP000007293; 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 14..300
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 355 AA; 38254 MW; C4C16E2A936E17E7 CRC64;
MMNGETNRPP ALGFSSDNIA GASPEVAQAI VKHSTGQASP YGTDELTAQV QRKFSEIFER
DVEVLLVPTG TSANGLCLSA MTPPWGNIYC HPASHINNDE CGAPEFFSNG AKLITIDGPS
AKLDITRLRE RTREKVGDVH TTQPACVSIT QATEVGSIYT LDEIAAIGDV CKSSSLGFHM
DGSRFANALV SLGCSPAEMT WKAGVDALSF GATKNGVLAA EAIVLFNTSL ANEMSYRRKR
AGHLFSKMRF LSAQIDAYLT DDLWLRNARQ ANAAAQRLAQ GLAGLNGVDV LGDTEANILF
CRLDPAIIEA LLRAGFGFYH DRWGPNIVRF VTSFATTAED VDHLLRQVRL ATRAD
//
