ID A0A3N0E853_9ACTN Unreviewed; 421 AA.
AC A0A3N0E853;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:RNL84018.1};
DE EC=4.2.3.1 {ECO:0000313|EMBL:RNL84018.1};
GN ORFNames=EFW17_14135 {ECO:0000313|EMBL:RNL84018.1};
OS Nocardiopsaceae bacterium YIM 96095.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae.
OX NCBI_TaxID=2487137 {ECO:0000313|EMBL:RNL84018.1, ECO:0000313|Proteomes:UP000269198};
RN [1] {ECO:0000313|EMBL:RNL84018.1, ECO:0000313|Proteomes:UP000269198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 96095 {ECO:0000313|EMBL:RNL84018.1,
RC ECO:0000313|Proteomes:UP000269198};
RA Tang S.-K., Chunyu W.-X., Feng Y.-Z.;
RT "The genome draft of YIM 96095.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR604450-51};
CC -!- SIMILARITY: Belongs to the threonine synthase family.
CC {ECO:0000256|ARBA:ARBA00005517}.
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:RNL84018.1}.
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DR EMBL; RJMB01000013; RNL84018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N0E853; -.
DR OrthoDB; 9778118at2; -.
DR Proteomes; UP000269198; Unassembled WGS sequence.
DR GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
DR CDD; cd01563; Thr-synth_1; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR004450; Thr_synthase-like.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR00260; thrC; 1.
DR PANTHER; PTHR48078:SF6; ACT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:RNL84018.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000269198}.
FT DOMAIN 88..391
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 122
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 421 AA; 44489 MW; 5D67657E6660CE42 CRC64;
MVMTATESST SAARSFGPAV ALSCRECGQR YALGPRFACE QCFGPLEVAY EFGDVSRESI
ARGPNNIWRY ADLLPVPDNV ADLPNMNPGL TPLVRADRLA AEVGMRSLHV KDDSGNPTHS
FKDRVVAMAV EAGRTFGFTT LSCSSTGNLA GAVGAAAARA GFRSCVFIPA GLEEGKIVMA
AVYGGQLVAI DGTYDDVNRF CSELIGDPAG EDWGFVNVNL RPYYAEGSKT LAYEIAEQLG
WRLPEQIIVP IASGSQLTKI DKGFRDLVKL GLVEDRPYRI FGAQATGCSP VARAWENGHD
VVQPMKPDTI AKSLAIGNPA DGPYVLDVCQ RTGGSVVHVS DAEIVDSIKL LARTEGVFAE
TAGGVTTGVL RKLIAEDGLD PQAETVVLNT GDGLKTLNAV DSGVTATIKP SLDAFKDAGL
L
//
