ID   A0A1V2YJJ6_9FIRM        Unreviewed;       484 AA.
AC   A0A1V2YJJ6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Threonine synthase {ECO:0000313|EMBL:OOB79718.1};
GN   ORFNames=BEN18_03295 {ECO:0000313|EMBL:OOB79718.1};
OS   Epulopiscium sp. Nuni2H_MBin001.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Candidatus Epulonipiscium.
OX   NCBI_TaxID=1884656 {ECO:0000313|EMBL:OOB79718.1, ECO:0000313|Proteomes:UP000189057};
RN   [1] {ECO:0000313|Proteomes:UP000189057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) 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:OOB79718.1}.
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DR   EMBL; MDJM01000006; OOB79718.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V2YJJ6; -.
DR   STRING; 1884656.BEN18_03295; -.
DR   Proteomes; UP000189057; Unassembled WGS sequence.
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; PTHR43515; THREONINE SYNTHASE-LIKE 1; 1.
DR   PANTHER; PTHR43515:SF1; THREONINE SYNTHASE-LIKE 1; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189057}.
FT   DOMAIN          3..79
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          104..400
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   484 AA;  53878 MW;  99B0BD21F3222024 CRC64;
     MLYESTRGDK TRIPAAQAIV KGLATDRGLY TPSFIPTLSD EEIVTIATSD YKDVAKLVFS
     KFLTDFSADE IDACIKGAYE NTFDTPEIAP LQQLDDNTSI LELWHGPTCA FKDVALQALP
     YLLTTSMKIT GESNKIAIIV ATSGDTGKAA LEGFKDVEGT SIVVMYPSEG VSLVQKQQMI
     TQQGENVNVI AIKGNFDDAQ TAAKNIFTNP DLEQQLLDKE IKLSSANSIN WGRLLPQIVY
     YIKSSLDIET DKLIDYVVPT GNFGNILAGY YAKKMGAPIG KLICASNSNN VLTDFIKTGV
     YDRRREFVKT LSPSMDILIS SNLERFLFEL SDHDSDLIDS LMNKLDLQGY YEIPQQLKLK
     MQGLLEAEYC TDQQTQEAIK QCWDKYNYLL DTHTAVAYNV HQMNKSDNPT IIVSTASPFK
     FPQGVYTALN GEVDLTEYQI LKELSNFTKW DIPAPIKDLE NIPVLHNTVC DKKEIVDTII
     GVIN
//