ID A0A1B1MEK7_STRLN Unreviewed; 402 AA.
AC A0A1B1MEK7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=L-allo-threonine aldolase {ECO:0000313|EMBL:ANS67001.1};
GN ORFNames=SLCG_4718 {ECO:0000313|EMBL:AXG55873.1}, SLINC_4777
GN {ECO:0000313|EMBL:ANS67001.1};
OS Streptomyces lincolnensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1915 {ECO:0000313|EMBL:ANS67001.1, ECO:0000313|Proteomes:UP000092598};
RN [1] {ECO:0000313|EMBL:ANS67001.1, ECO:0000313|Proteomes:UP000092598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2936 {ECO:0000313|EMBL:ANS67001.1,
RC ECO:0000313|Proteomes:UP000092598};
RA Meng S.C.;
RT "Enhancement of antibiotic productionsby engineered nitrateutilization in
RT actinobacteria.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AXG55873.1, ECO:0000313|Proteomes:UP000253884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC-G {ECO:0000313|EMBL:AXG55873.1,
RC ECO:0000313|Proteomes:UP000253884};
RX PubMed=29574602; DOI=10.1007/s10295-018-2029-1;
RA Xu Y., Tan G., Ke M., Li J., Tang Y., Meng S., Niu J., Wang Y., Liu R.,
RA Wu H., Bai L., Zhang L., Zhang B.;
RT "Enhanced lincomycin production by co-overexpression of metK1 and metK2 in
RT Streptomyces lincolnensis.";
RL J. Ind. Microbiol. Biotechnol. 45:345-355(2018).
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}.
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DR EMBL; CP016438; ANS67001.1; -; Genomic_DNA.
DR EMBL; CP022744; AXG55873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B1MEK7; -.
DR STRING; 1915.SLINC_4777; -.
DR KEGG; sls:SLINC_4777; -.
DR PATRIC; fig|1915.4.peg.5310; -.
DR Proteomes; UP000092598; Chromosome.
DR Proteomes; UP000253884; Chromosome.
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 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:SF9; L-THREONINE ALDOLASE; 1.
DR PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 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:UP000092598}.
FT DOMAIN 79..306
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..46
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 44095 MW; 74DC78D50210C7DA CRC64;
MIPGMSDTAE QGEGRTGPES DDERRARQRE RRIGAHRSAR RVLARSGHQR TLRERLDLLE
RAADVYDLDE LSDLYGGGVV EALEEKVAGL LGKEAAVFFP TGTMAQQVAL RCWAGRTGNP
TVALHALAHP EVHERNAFSQ VSGLRPVRVT SEPRMPTAAE VRDLDEPFGA LMLELPLRDA
GHLLPSWEEL TEVVEAARER EAVVHFDGAR LWEATVHLGR PLDEIADLAD SVYVSFYKSL
GGYGGAVLAG PRALTEEARA WRHRYGGTVY QQFPTVLSAL VGLERELPRL PDYVRHARVV
AAALREGFAA AGVPWARVHP EVPHTNEFQV WLPYDAETAT EAAVRQTEET GTELFGRPWG
TPGPGLAVTE ISVRAESLEW TPDDVKAAVT DFVARVTGAD GL
//
