ID   A0A1E4L287_9PROT        Unreviewed;       474 AA.
AC   A0A1E4L287;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Threonine synthase {ECO:0000313|EMBL:ODU48592.1};
GN   ORFNames=ABS92_08070 {ECO:0000313|EMBL:ODU48592.1};
OS   Thiobacillus sp. SCN 63-374.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=1660149 {ECO:0000313|EMBL:ODU48592.1, ECO:0000313|Proteomes:UP000094238};
RN   [1] {ECO:0000313|EMBL:ODU48592.1, ECO:0000313|Proteomes:UP000094238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA   Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA   Banfield J.F.;
RT   "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT   unravelled with genome-resolved metagenomics.";
RL   Environ. Microbiol. 17:4929-4941(2015).
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:ODU48592.1}.
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DR   EMBL; MEFK01000098; ODU48592.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4L287; -.
DR   Proteomes; UP000094238; 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; 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};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51}.
FT   DOMAIN          2..79
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          110..339
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         120
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   474 AA;  52153 MW;  1D9EAEB06CCEE131 CRC64;
     MNYLSTRGLA PQLRFSEILL GGLASDGGLY VPETYPRFSD AELTVMREMD YRELAFAVLS
     RLIDDIPHDD LRRLIDKTYT ADVYRYAGPG ENAADITPLK TLEPGLHVLA LSNGPTLAFK
     DMAMQLLGNL FEYVLTKTGG ELNILGATSG DTGSAAEYAM RGKRGIRVFM LSPEHGMTRF
     QQAQMYALTD ANIHNLVIRG VFDQCQDIVK AVSNDLAFKK AHRIGAVNSI NWARVAAQSV
     YYFKAYFAAT QSNDQQVSFS VPSGNFGNVC AGHIARRMGL PIAKLIVATN ENDVLDEFFK
     TGVYRPRPET RHTSSPSMDI SKASNFERFV FDLAGRDAAR IRSLWGAVES GGSFDLNADG
     LFRRVAEFGM VSGSSSHANR IDTIRTVYEV YGTMIDPHTA DGLKVGLEHR EPGVPLICME
     TAQPAKFEDA IREALGIEPV RPAELAELEA QPQKKHVMDA DIDAVKQFIV DHAG
//