ID A0A074TH52_9RHOB Unreviewed; 355 AA.
AC A0A074TH52;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=L-threonine aldolase {ECO:0000256|PIRNR:PIRNR038940};
DE EC=4.1.2.48 {ECO:0000256|PIRNR:PIRNR038940};
GN ORFNames=DL1_10095 {ECO:0000313|EMBL:KEP70994.1};
OS Thioclava dalianensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1185766 {ECO:0000313|EMBL:KEP70994.1, ECO:0000313|Proteomes:UP000027725};
RN [1] {ECO:0000313|EMBL:KEP70994.1, ECO:0000313|Proteomes:UP000027725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DLFJ1-1 {ECO:0000313|EMBL:KEP70994.1,
RC ECO:0000313|Proteomes:UP000027725};
RA Lai Q., Shao Z.;
RT "The draft genome sequence of Thioclava dalianensis DLFJ1-1.";
RL Submitted (MAR-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 -!- 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:KEP70994.1}.
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DR EMBL; JHEH01000003; KEP70994.1; -; Genomic_DNA.
DR RefSeq; WP_038062352.1; NZ_JHEH01000003.1.
DR AlphaFoldDB; A0A074TH52; -.
DR STRING; 1185766.SAMN05216224_103275; -.
DR eggNOG; COG2008; Bacteria.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000027725; 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:UP000027725}.
FT DOMAIN 3..292
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 355 AA; 37766 MW; 2D0731EDA6DF5979 CRC64;
MNFASDNTSG AHPRIMEALA AANEGHVPSY GADPRTQAVE ARLREIFEAP EARVYLVATG
SAANALSCAV LTDPWGAIFC HRNAHIEEDE CGAPEFYTGG SKLVLVDGAD AKMDPGALQR
TIAHTGRGGI HNVQRGMVSI TNATEAGAVY TPAEVSALSA IARQFELPVH MDGARFANAL
IAAGCTPAEM TWKAGVDVLS FGGTKNGCMG VEAVVIFDPK RAWEFELRRK RGGHLFSKHR
FLAAQMQAYL EGDLWLSLAT HANEMAAKLS SGIVEAPGAK LVHPTQANAV FASLPRGAHR
RAQGAGAYYY LWPFDQSLEG APEELLAARL VCSWATTPDE IDVFLGYLNG GSTPG
//
