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Database: UniProt
Entry: A0A073AZ43_9PSEU
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ID   A0A073AZ43_9PSEU        Unreviewed;       338 AA.
AC   A0A073AZ43;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:KEI44620.1};
GN   ORFNames=GU90_08905 {ECO:0000313|EMBL:KEI44620.1};
OS   Saccharopolyspora rectivirgula.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=28042 {ECO:0000313|EMBL:KEI44620.1, ECO:0000313|Proteomes:UP000031419};
RN   [1] {ECO:0000313|EMBL:KEI44620.1, ECO:0000313|Proteomes:UP000031419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43113 {ECO:0000313|EMBL:KEI44620.1,
RC   ECO:0000313|Proteomes:UP000031419};
RA   Barrera C., Millon L., Rognon B., Zaugg C., Monod M.;
RT   "Saccharopolyspora rectivirgula DSM-43113 Genome sequencing.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the threonine aldolase family.
CC       {ECO:0000256|ARBA:ARBA00006966}.
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:KEI44620.1}.
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DR   EMBL; JNVU01000024; KEI44620.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A073AZ43; -.
DR   STRING; 28042.GU90_08905; -.
DR   eggNOG; COG2008; Bacteria.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000031419; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR023603; Low_specificity_L-TA-like.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; NF041359; GntG_guanitoxin; 1.
DR   PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF017617; Thr_aldolase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000031419}.
FT   DOMAIN          8..292
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         207
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   338 AA;  35552 MW;  3636955989DA4AA5 CRC64;
     MTKPEPIDLR SDTVTRPDQQ MSAAMATAEV GDDVLDHDPT MRALEERVAH LLGMPAALWV
     PSGTMGNLIA LCLHLGRGQR FLAPRGAHVL THELGSAAWL AGGMPDPLPW DAGPGRPAPE
     TVRANVEAEA PYDSLRTTLL CLENTHNEAG GAVVPPDEHA KLVSAARDAG LRVHLDGARI
     WNAAVALEVP PAALTAGVDS VQACLSKGLG APVGSVVAGS TNFIAEARRM RKMLGGGVRQ
     GGVLAAAGLV ALDRIDSLAE DHRKAARLAR GLAELGWKVT TPQTNMVLAE AADVRATVDR
     LAGVGVLAVP MGDRIRFVTH RDVSEADVER ALQRIAEF
//
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