ID A0A158G1Q0_9BURK Unreviewed; 344 AA.
AC A0A158G1Q0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=L-threonine aldolase {ECO:0000256|PIRNR:PIRNR038940};
DE EC=4.1.2.48 {ECO:0000256|PIRNR:PIRNR038940};
GN ORFNames=AWB69_01925 {ECO:0000313|EMBL:SAL25853.1};
OS Caballeronia udeis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=1232866 {ECO:0000313|EMBL:SAL25853.1, ECO:0000313|Proteomes:UP000054683};
RN [1] {ECO:0000313|EMBL:SAL25853.1, ECO:0000313|Proteomes:UP000054683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 27134 {ECO:0000313|EMBL:SAL25853.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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 -!- SIMILARITY: Belongs to the threonine aldolase family.
CC {ECO:0000256|ARBA:ARBA00006966, ECO:0000256|PIRNR:PIRNR038940}.
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DR EMBL; FCOK02000009; SAL25853.1; -; Genomic_DNA.
DR RefSeq; WP_062084621.1; NZ_FCOK02000009.1.
DR AlphaFoldDB; A0A158G1Q0; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000054683; 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 4..292
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 344 AA; 37456 MW; BF35F496E192D258 CRC64;
MQHFASDNYA GICPEALAAL IEANNSGHEP AYGDDSWTQG VCDRIRDLFQ TDCEVFFVFN
GTAANSLALA SLCQSYHSVI CHELAHIETD ECGGPEFFSG GSKLLTAPGI DGKLTPDAIE
AIVTRRADIH YPKPKVVTLT QSTEVGTVYS VEEIRAIAAI AKRRHLKVHM DGARFANAVA
SLNVHPSEIT WRAGVDVLCF GGTKNGLPVG EAVIFFDKAL AVDFAYRLKQ AGQLASKMRF
ISAPWLGLLN NDVWLRNARH ANGMAQLMAE RLEGIEGVKV MFRPQGNAVF AELPPAVAQA
LRNKGWKFYQ FIGSGGCRLM CAWDTLPETV EQFAGEVRVL CAAH
//