ID   Q2LS84_SYNAS            Unreviewed;       483 AA.
AC   Q2LS84;
DT   21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   21-FEB-2006, sequence version 1.
DT   10-JUN-2026, entry version 100.
DE   RecName: Full=Threonine synthase {ECO:0000256|NCBIfam:TIGR00260};
DE            EC=4.2.3.1 {ECO:0000256|NCBIfam:TIGR00260};
GN   ORFNames=SYN_02122 {ECO:0000313|EMBL:ABC76943.1};
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Pseudomonadati; Thermodesulfobacteriota; Syntrophia;
OC   Syntrophales; Syntrophaceae; Syntrophus.
OX   NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC76943.1, ECO:0000313|Proteomes:UP000001933};
RN   [1] {ECO:0000313|EMBL:ABC76943.1, ECO:0000313|Proteomes:UP000001933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB {ECO:0000313|EMBL:ABC76943.1,
RC   ECO:0000313|Proteomes:UP000001933};
RX   PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA   McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA   Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA   Campbell J.W., Gunsalus R.P.;
RT   "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT   of microbial growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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}.
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DR   EMBL; CP000252; ABC76943.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2LS84; -.
DR   FunCoup; Q2LS84; 320.
DR   STRING; 56780.SYN_02122; -.
DR   KEGG; sat:SYN_02122; -.
DR   eggNOG; COG0498; Bacteria.
DR   HOGENOM; CLU_015170_0_0_7; -.
DR   InParanoid; Q2LS84; -.
DR   Proteomes; UP000001933; Chromosome.
DR   GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009088; P:L-threonine biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR051166; Threonine_Synthase.
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:ABC76943.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001933}.
FT   DOMAIN          45..114
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          128..419
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         141
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   483 AA;  54242 MW;  1513BBE400535485 CRC64;
     MKVEFSVPRR REKLHRMGEF MRERILYYST NCYLDNVEGM EPFKDRVSFR EALLLGQAPD
     EGLFMPESIP QLSLDEILNL KGRPYTAAAL LVAEAYLGAD LPLETLKAVI ESSYNYEVPL
     ERVVDRRYVL RLDRGPTASF KDFAARMMAR LMSHFRDPGK RLNVLVATSG DTGSAVGEAF
     KGVAGIDVYI LYPREEVSGR QKKQLDTIGG NVRTLSVEGK FDDCQDLVKQ AFADPALAGL
     NLTSANSINF GRILPQMIYY VYAYAQLAER GEEIVFSVPS GNFGDALGCE YARRMGLPVA
     QLVMPTNEND EFPRFLKTGR YEKISPSLAC LSNAMNVGHP SNLARFFDLY GGTVDRTGRV
     HKMPDLEEMR NNIFSVSVSD EETRRTIRRA YDSYGLILEP HGAVGWRGLE LYLEQTGRKV
     LCVSLETAHP AKFPEEIVSL LGISPELPAS MRDIDSRTGE PLPMTGDYNV FRKFLEKTLK
     AMD
//