ID A0A176Z5G0_9BRAD Unreviewed; 358 AA.
AC A0A176Z5G0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=L-threonine aldolase {ECO:0000256|PIRNR:PIRNR038940};
DE EC=4.1.2.48 {ECO:0000256|PIRNR:PIRNR038940};
GN ORFNames=AYJ54_41210 {ECO:0000313|EMBL:OAF14982.1};
OS Bradyrhizobium centrolobii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1505087 {ECO:0000313|EMBL:OAF14982.1, ECO:0000313|Proteomes:UP000076959};
RN [1] {ECO:0000313|EMBL:OAF14982.1, ECO:0000313|Proteomes:UP000076959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR 10245 {ECO:0000313|EMBL:OAF14982.1,
RC ECO:0000313|Proteomes:UP000076959};
RA Simoes-Araujo J.L.Sr., Barauna A.C., Silva K., Zilli J.E.;
RT "Draft Genome Sequence of the Strain BR 10245 (Bradyrhizobium sp.) isolated
RT from nodules of Centrolobium paraense.";
RL Submitted (MAR-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}.
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:OAF14982.1}.
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DR EMBL; LUUB01000026; OAF14982.1; -; Genomic_DNA.
DR RefSeq; WP_063696946.1; NZ_LUUB01000026.1.
DR AlphaFoldDB; A0A176Z5G0; -.
DR STRING; 1505087.AYJ54_41210; -.
DR Proteomes; UP000076959; 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 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 17..307
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 358 AA; 38230 MW; 68C4F05C6EC072E0 CRC64;
MTAGQDGINE AARTLPNFRS DNVAPVRPEI LQAIAEANRG PAAAYGDDDY SKLLNRRFST
LFETEVTVFP VSTGTAANAL SLASCARPYG AVYCHEEAHI HTAEGGATEA FTGGAKLLPM
PGPHFRIEPS NLREALASAG WGVRNRAQPD AISITQASEY GTIYPLAEIA EIGAIAHDKN
LSLHMDGARF ANALARLGCS PADMTWRAGV DILSFGATKN GAMSADAIVV FDQDLVESLS
YRLRRAGQTA SKMRYASAQL LAYVEDRLYL RLAAKANAVA ARLGAGLAAL PDVRLVAPVE
ANLVFLNLPG QAINRLAAIG LHFARRGHDV IRFVARFDST EQEADELIAL VRSAVTRS
//
