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Database: UniProt
Entry: A0A413G8M1_9FIRM
LinkDB: A0A413G8M1_9FIRM
Original site: A0A413G8M1_9FIRM 
ID   A0A413G8M1_9FIRM        Unreviewed;       497 AA.
AC   A0A413G8M1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   ORFNames=DWV16_01635 {ECO:0000313|EMBL:RGX57044.1};
OS   Anaerotruncus sp. AF02-27.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Anaerotruncus.
OX   NCBI_TaxID=2292191 {ECO:0000313|EMBL:RGX57044.1, ECO:0000313|Proteomes:UP000284135};
RN   [1] {ECO:0000313|EMBL:RGX57044.1, ECO:0000313|Proteomes:UP000284135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF02-27 {ECO:0000313|EMBL:RGX57044.1,
RC   ECO:0000313|Proteomes:UP000284135};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-homoserine = L-threonine + phosphate;
CC         Xref=Rhea:RHEA:10840, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57590, ChEBI:CHEBI:57926; EC=4.2.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000051};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR604450-51};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 5/5. {ECO:0000256|ARBA:ARBA00004979}.
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:RGX57044.1}.
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DR   EMBL; QSBX01000001; RGX57044.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A413G8M1; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000284135; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
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.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Lyase {ECO:0000313|EMBL:RGX57044.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000284135};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          2..79
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          103..316
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         113
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   497 AA;  53668 MW;  C5C747E2641BA271 CRC64;
     MNYISTRDSG YAVSSAQAIV AGLAPDGGLF LPETLPEYTA GELETLTKSG YTARATSILS
     RFLPDFTREE LHQYVCRAYA PEKFPPKAVA PVVPLDENAS ILELFHGPTC AFKDFALQLL
     PFLLTASLQK TGEDKTVVIL VATSGDTGKA ALEGFADVEG TKICVFYPDG GTSNIQRLQM
     TTQQGNNVMV FAAKGNFDDA QNGVKRIFTD QDFASLLAEK GFVLSSANSI NWGRLVPQVA
     YYFSAYCDLV NAGRIKLGDK INVVVPTGNF GNILAAYFAK HCGLPVGKLI CASNKNNVLT
     DFITTGTYDR NRDFYVTSSP SMDILISSNL ERLLYLLCDR DDGKLKGYMN ELSATGKYTV
     DKTILEKLQS EFAAGCADDK QTAETIASVY EKTHYLCDTH TAVAVKVYQD YAAKTGDTTP
     TVIASTASPF KFAGSVLPAI GKAPSGGDFE LLRELSEATG LQAPAALAGL RDRKERFTDV
     VEPTKMKDAV AAWLGVK
//
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