ID A0A367XY97_9MICO Unreviewed; 469 AA.
AC A0A367XY97;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:RCK58597.1};
DE EC=4.2.3.1 {ECO:0000313|EMBL:RCK58597.1};
GN ORFNames=DTO57_10595 {ECO:0000313|EMBL:RCK58597.1};
OS Microbacterium sorbitolivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1867410 {ECO:0000313|EMBL:RCK58597.1, ECO:0000313|Proteomes:UP000253508};
RN [1] {ECO:0000313|EMBL:RCK58597.1, ECO:0000313|Proteomes:UP000253508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C1.15228 {ECO:0000313|EMBL:RCK58597.1,
RC ECO:0000313|Proteomes:UP000253508};
RA An D.;
RT "Microbacterium endoborsara sp. nov., a novel actinobacterium isolated from
RT Borszczowia aralocaspica.";
RL Submitted (JUL-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:RCK58597.1}.
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DR EMBL; QORO01000003; RCK58597.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367XY97; -.
DR OrthoDB; 9778118at2; -.
DR Proteomes; UP000253508; 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; cd01560; Thr-synth_2; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.90.1380.10; Threonine synthase, N-terminal domain; 1.
DR InterPro; IPR029144; Thr_synth_N.
DR InterPro; IPR037158; Thr_synth_N_sf.
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; PTHR42690; THREONINE SYNTHASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42690:SF1; THREONINE SYNTHASE-LIKE 2; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF14821; Thr_synth_N; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:RCK58597.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000253508}.
FT DOMAIN 2..79
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 106..313
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 112
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 469 AA; 50957 MW; 17809C96E3A56125 CRC64;
MQYISTRGGM EPTEFCETLL EGLAPDGGLA IPTQLPSVDA STLEAWRGLD YADLATEVIG
LFATDIPRDD LSAMTHAAYS ADKFPGGIVP LRDIDGGITL VGLSEGPTLA FKDMAMQFLG
QVMEYALERR GTTLNIVGAT SGDTGSAAEQ AFRGKKHINV FMLSPQGRMS GFQRAQMFSL
QDENIHNIAV EGVFDDAQNL VKALSGDLEF KRAHNLGAVN SINLARIVAQ VVYYFWAWLR
ATDNRGVLEV SVAVPSGNFG NILAGYFAKS MGLPIRKLVL AANENNVLDE FFRTGLYRPR
SSEQTLATSS PSMDISKASN LERFLFDLLG RDAARMNAAW AELDANGVLD LTAELPRLTG
EFGFGSGTST HADRLATIKA VYKATGEIID PHTADGVKVA RDYVEEGVPM LVMETAKPAK
FQETITEAIG VEIELNDELR AMLDAPQRVV EMPSDEQLLR YYVSKHAAL
//
