ID   A0A101V9K7_9FIRM        Unreviewed;       494 AA.
AC   A0A101V9K7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Threonine synthase {ECO:0000313|EMBL:KUO50470.1};
GN   ORFNames=APF76_07375 {ECO:0000313|EMBL:KUO50470.1};
OS   Desulfitibacter sp. BRH_c19.
OC   Bacteria; Bacillota; Clostridia; Moorellales; Desulfitibacteraceae;
OC   Desulfitibacter.
OX   NCBI_TaxID=1734395 {ECO:0000313|EMBL:KUO50470.1, ECO:0000313|Proteomes:UP000053015};
RN   [1] {ECO:0000313|EMBL:KUO50470.1, ECO:0000313|Proteomes:UP000053015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c19 {ECO:0000313|EMBL:KUO50470.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
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         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:KUO50470.1}.
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DR   EMBL; LOER01000032; KUO50470.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101V9K7; -.
DR   STRING; 1734395.APF76_07375; -.
DR   Proteomes; UP000053015; 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}.
FT   DOMAIN          6..80
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          105..408
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   494 AA;  55259 MW;  6010273215C39BC4 CRC64;
     MSNIYYSSTR GNHEKLTFSE AVVKGIAPDG GLYVPSKFPK LVFNDDLLNL SYQDLAKKIL
     SLYIEDFSIE EISYCVDHAY DSKFRELLIA PIETLDKASF IELYHGKTLA FKDMALSILP
     YLLKTASKKL AIKEKIVILT ATSGDTGKAA LEGFADVDGI EIIVFYPTKG VSDVQKRQMT
     TQGGANVTVL GITGNFDDAQ NGVKDIFLDE ELREELKSKG YTFSSANSIN IGRLLPQIVY
     YVHSYLMLVK EGHIKNGDLI NIVVPTGNFG NILAAYYAKN MGLPVQKFIC ASNTNNVLTD
     FLNTGVYDIH RKFEMTNTPS MDILISSNLE RFLYEISNRD SACVTSLMKS LKQDGRYEIT
     INMKNNLAAF SGGFATDEET VEAIRFLYSQ YNYVADTHTA VGFKVYQDYV DETADMTHTL
     IASTASPYKF TRSVVEGLGM QTEAYNDFEL IDILSNATHI NVPEPIKDIQ DKQILHPRVI
     DKNNLKKEVV EILK
//