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Database: UniProt
Entry: A0A117Q388_9ACTN
LinkDB: A0A117Q388_9ACTN
Original site: A0A117Q388_9ACTN 
ID   A0A117Q388_9ACTN        Unreviewed;       356 AA.
AC   A0A117Q388;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:KUN06101.1};
GN   ORFNames=AQI95_14420 {ECO:0000313|EMBL:KUN06101.1};
OS   Streptomyces yokosukanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67386 {ECO:0000313|EMBL:KUN06101.1, ECO:0000313|Proteomes:UP000053127};
RN   [1] {ECO:0000313|EMBL:KUN06101.1, ECO:0000313|Proteomes:UP000053127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40224 {ECO:0000313|EMBL:KUN06101.1,
RC   ECO:0000313|Proteomes:UP000053127};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces yokosukanensis DSM 40224, type
RT   strain for the species Streptomyces yokosukanensis.";
RL   Submitted (OCT-2015) 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:KUN06101.1}.
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DR   EMBL; LMWN01000018; KUN06101.1; -; Genomic_DNA.
DR   RefSeq; WP_067122430.1; NZ_KQ948210.1.
DR   AlphaFoldDB; A0A117Q388; -.
DR   STRING; 67386.AQI95_14420; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000053127; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
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; 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   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053127}.
FT   DOMAIN          19..306
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   356 AA;  39220 MW;  89011908D7411B86 CRC64;
     MNPPKTDARR HHDPQVRGFA SDNYAGAHPE VLAALAVANG GHQVAYGEDE YTENLQRIIR
     GHFGSTAEAF PVFNGTGANV VALQAVTDRW GAVICAESAH INVDEGGAPE RMGGLKLLTV
     PTPDGKLTPE LIDRQAWGFE DEHRAMPQVV SITQSTELGT RYTPEEIRAI CEHAHARGMR
     VHLDGSRIAN AAASLNVPMR TFTNAVGVDI LSLGGTKNGA VFGEAVVVIN QDAVRQMKHL
     RKMSMQLASK MRFVSVQLEA LLSKDLWLRN ARHANEMAQR LAEGVRAVHG VEILYPVQAN
     GVFAKLPHDV SERLQKRFRF YFWDEAAGTV RWMCSFDTTE EDVDTFVAAL KEEMAR
//
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