ID   A0A3A9UP73_9FLAO        Unreviewed;       432 AA.
AC   A0A3A9UP73;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   ORFNames=D1817_14715 {ECO:0000313|EMBL:AXT21074.1};
OS   Flavobacteriaceae bacterium.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1871037 {ECO:0000313|EMBL:AXT21074.1, ECO:0000313|Proteomes:UP000260281};
RN   [1] {ECO:0000313|EMBL:AXT21074.1, ECO:0000313|Proteomes:UP000260281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU392 {ECO:0000313|EMBL:AXT21074.1,
RC   ECO:0000313|Proteomes:UP000260281};
RA   Song W., Thomas T., Edwards R.;
RT   "Complete genome sequences of pooled genomic DNA from 10 marine bacteria
RT   using PacBio sequencing.";
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}.
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DR   EMBL; CP031964; AXT21074.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A9UP73; -.
DR   OrthoDB; 9763107at2; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000260281; Chromosome.
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   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; 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.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AXT21074.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000260281};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          3..79
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          94..373
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         107
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   432 AA;  48211 MW;  4833543BC2A105E3 CRC64;
     MDYFSLNYNA PKVSFKEAVI KGLAPDKGLY FPSEINPLPK SFFDTIESLD NTSIAFEVIK
     QFVGNNIPSV DLKALIKDTL SFNFPIVKIE GNIVALELYH GPTMAFKDVG ARFMARCLGY
     FNKNKFSREK ITVLVATSGD TGGAVASGFL DVEGVEVVIL YPSGKVSDIQ EKQLTTLGKN
     ITALEVNGTF DDCQSMVKEA FLDVDYNGVK TLTSANSINV ARWLPQMFYF FFAYKELKSL
     NKKLVFSVPS GNYGNICAGM MAQKLGLPIH HFVAGTNINN VVPSYLETGK YNPKSSIQTI
     SNAMDVGAPS NFIRIKHLYQ NNIKLLQEHL SGYSYTDDDT IEGIKYLFET NNYISDPHGT
     IGYLALRDYL KDKENIQGVF LETAHPIKFL DVMPAKIADS LPIPSQISEI MSRSKRSIQI
     KNYKDLKEYL LQ
//