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Database: UniProt
Entry: A0A101T4B7_9ACTN
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ID   A0A101T4B7_9ACTN        Unreviewed;       347 AA.
AC   A0A101T4B7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=L-threonine aldolase {ECO:0000256|PIRNR:PIRNR038940};
DE            EC=4.1.2.48 {ECO:0000256|PIRNR:PIRNR038940};
GN   ORFNames=AQJ64_10695 {ECO:0000313|EMBL:KUN85593.1};
OS   Streptomyces griseoruber.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1943 {ECO:0000313|EMBL:KUN85593.1, ECO:0000313|Proteomes:UP000052982};
RN   [1] {ECO:0000313|EMBL:KUN85593.1, ECO:0000313|Proteomes:UP000052982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40281 {ECO:0000313|EMBL:KUN85593.1,
RC   ECO:0000313|Proteomes:UP000052982};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces griseoruber DSM 40281, type strain
RT   for the species Streptomyces griseoruber.";
RL   Submitted (OCT-2015) 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:KUN85593.1}.
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DR   EMBL; LMWW01000012; KUN85593.1; -; Genomic_DNA.
DR   RefSeq; WP_055637510.1; NZ_LIQS01000508.1.
DR   AlphaFoldDB; A0A101T4B7; -.
DR   STRING; 1943.AQJ64_10695; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000052982; Unassembled WGS sequence.
DR   GO; GO:0008732; F:L-allo-threonine aldolase activity; IEA:RHEA.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
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          8..294
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   347 AA;  36488 MW;  292041A1D3E518A7 CRC64;
     MTLPARIFSS DNTAGASPEI VEAVSRAAAG QAQPYGADDL TAGVRHRLGE VFEREVDVLL
     VSSGTAANAL SLAALTPPWG SVLCHRDSHI NNDECGAPEF YTAGAKLVPL GGEDAKIDPG
     ELRAAVRHKA GDVHSVEPSV VSLTQATETG AVYTPDEIGT LGSLAEEAGL RLHMDGARFA
     GAVAALGRTP AELTWRAGVD LLSFGATKNG TMTADAIVVF DRSLTPELSF RAKRAGQLAA
     KTRFHAAQVD AYLTDGLWLR NAAHANGMAA RLQDGLKALP EVGLLGVADA NIVFCRLPRQ
     VTEGLLGEGY VFYHDRWEPG VARFVTSFAT TEADVDGLLA AVRRYAG
//
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