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Database: UniProt
Entry: A0A117RRK5_9ACTN
LinkDB: A0A117RRK5_9ACTN
Original site: A0A117RRK5_9ACTN 
ID   A0A117RRK5_9ACTN        Unreviewed;       356 AA.
AC   A0A117RRK5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:KUO05362.1};
GN   ORFNames=AQJ67_08325 {ECO:0000313|EMBL:KUO05362.1};
OS   Streptomyces caeruleatus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=661399 {ECO:0000313|EMBL:KUO05362.1, ECO:0000313|Proteomes:UP000053429};
RN   [1] {ECO:0000313|EMBL:KUO05362.1, ECO:0000313|Proteomes:UP000053429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-24802 {ECO:0000313|EMBL:KUO05362.1,
RC   ECO:0000313|Proteomes:UP000053429};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces caeruleatus NRRL B-24802, type
RT   strain for the species Streptomyces caeruleatus.";
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:KUO05362.1}.
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DR   EMBL; LMWY01000005; KUO05362.1; -; Genomic_DNA.
DR   RefSeq; WP_062717392.1; NZ_KQ948925.1.
DR   AlphaFoldDB; A0A117RRK5; -.
DR   STRING; 661399.AQJ67_08325; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000053429; 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:UP000053429}.
FT   DOMAIN          19..306
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   356 AA;  38944 MW;  183C72E178B73556 CRC64;
     MNPPKTDARR HHDPDVRGFA SDNYAGAHPE VLAALALANG GHQVAYGEDD YTENLQRIVR
     SHFGATAEAF PVFNGTGANV VALQAVTDRW GAVICAESAH IHVDEGGAPE RMGGLKLLTV
     PTPDGKLTPE LIDKQAYGWD DEHRAMPQVV SITQSTELGT LYTPDEIRAI CDHAHAHGMK
     VHLDGSRIAN AAASLNVPMR TFTNAVGVDI LSLGGTKNGA LFGEAVVVLN QDAVSHMKHL
     RKLSMQLASK MRFVSVQLEA LLAKDLWLRN ARHANEMAQR LAEGVRAVHG VEILYPVQAN
     GVFAKLPHDV SERLQKRFRF YFWDEAAGVV RWMCAFDTTE DDVDAFVAAL KEEMAR
//
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