ID   A0A411WMM2_9GAMM        Unreviewed;       429 AA.
AC   A0A411WMM2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   ORFNames=EKN56_14260 {ECO:0000313|EMBL:QBH97464.1};
OS   Limnobaculum zhutongyuii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Budviciaceae; Limnobaculum.
OX   NCBI_TaxID=2498113 {ECO:0000313|EMBL:QBH97464.1, ECO:0000313|Proteomes:UP000293154};
RN   [1] {ECO:0000313|EMBL:QBH97464.1, ECO:0000313|Proteomes:UP000293154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF-458 {ECO:0000313|EMBL:QBH97464.1,
RC   ECO:0000313|Proteomes:UP000293154};
RA   Ge Y.;
RT   "Pragia sp. nov. isolated from the gut tract of Carduelis flavirostris.";
RL   Submitted (MAR-2019) 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; CP034752; QBH97464.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A411WMM2; -.
DR   KEGG; prag:EKN56_14260; -.
DR   OrthoDB; 9763107at2; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000293154; 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:QBH97464.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          8..80
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          96..369
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   429 AA;  46571 MW;  2ED3498363473197 CRC64;
     MKLYNLKDHN EQVSFAQAVR QGLGKQQGLF FPADLPAFDS SEIDNLLSLD FVTRSARILS
     AYIGDEISAD AVAKRVANAF QFPAPVVAVE KDIATLELFH GPTLAFKDFG GRIMAQMLAE
     VAGDTPVTIL TATSGDTGAA VAHAFYGLKN VRVVILYPEG KISPLQEKLF CTLGGNIHTV
     AVDGDFDACQ ALVKQAFDDE VLKKELGLNS ANSINISRLL AQICYYFEAV AQLTQEQHNQ
     LVISVPSGNF GDLTAGLLAK SLGLPVKRFI AATNANDTVP RYLANGQWQP HKTVATLSNA
     MDVSQPNNWP RIEELFRRKE WPVSSLGYGA VSDETTAKTL RELAALGYTS EPHGAIAYRL
     LRDELKDGEF GLFLGTAHPA KFKESVEQIL GTTLPLPKAL ADRAELPLLS HYLPADFAPL
     RAFLMALPA
//