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Entry: A0A0N8K827_9SPHN
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ID   A0A0N8K827_9SPHN        Unreviewed;       477 AA.
AC   A0A0N8K827;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   Name=thrC {ECO:0000313|EMBL:KPP93369.1};
GN   ORFNames=HLUCCO15_06105 {ECO:0000313|EMBL:KPP93369.1};
OS   Erythrobacteraceae bacterium HL-111.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae.
OX   NCBI_TaxID=1666908 {ECO:0000313|EMBL:KPP93369.1, ECO:0000313|Proteomes:UP000050295};
RN   [1] {ECO:0000313|EMBL:KPP93369.1, ECO:0000313|Proteomes:UP000050295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-111 {ECO:0000313|EMBL:KPP93369.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-2015) 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:KPP93369.1}.
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DR   EMBL; LJSW01000009; KPP93369.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N8K827; -.
DR   PATRIC; fig|1666908.3.peg.2817; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000050295; 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; 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};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          2..80
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          87..329
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         112
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   477 AA;  51416 MW;  8451D58105CA830F CRC64;
     MEYLSTRGSA PALDFEGVTL AGLASDGGLY LPREWPRFSP EEIRAMRGLS YADIAARVMQ
     PFVEGSLTAG ELSAICHEVY GEFGHAAVTP LVQLDERHWL LELFHGPTLA FKDVALQLLG
     RLFETFLDRR GERLTIVGAT SGDTGSAAIR AVAGLERVEI FMLHPKGRVS EVQRRQMTTV
     RAPNVHNLAI EGSFDDAQAH VKRMFGDPAI NGPLALGAVN SINWARLMAQ VVYYFASALQ
     LGAPDRPVAY SVPTGNFGDV FAGYVAAKMG LPVERLIVAT NVNDILHRAL TSGDYSAGDV
     TATHTPSMDI QVSSNFERLL FDCGGRDGAA MAEQMRGFET ARAMQLTNAQ REGAAALFTS
     CRADQDDTAR ALQWAWRQAG QVIDPHTGVG LHASLACAAK GAVEPGTPLV TLATAHPAKF
     REAVERAIGV RPNLPGRVGD LFAREESFTE LPGDYEASRD FVLEHALART DADPAEA
//
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