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Database: UniProt
Entry: T0J7T6_9SPHN
LinkDB: T0J7T6_9SPHN
Original site: T0J7T6_9SPHN 
ID   T0J7T6_9SPHN            Unreviewed;       414 AA.
AC   T0J7T6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   ORFNames=M529_01490 {ECO:0000313|EMBL:EQB34026.1};
OS   Sphingobium ummariense RL-3.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1346791 {ECO:0000313|EMBL:EQB34026.1, ECO:0000313|Proteomes:UP000015523};
RN   [1] {ECO:0000313|EMBL:EQB34026.1, ECO:0000313|Proteomes:UP000015523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RL-3 {ECO:0000313|EMBL:EQB34026.1,
RC   ECO:0000313|Proteomes:UP000015523};
RX   PubMed=24233594;
RA   Kohli P., Dua A., Sangwan N., Oldach P., Khurana J.P., Lal R.;
RT   "Draft Genome Sequence of Sphingobium ummariense Strain RL-3, a
RT   Hexachlorocyclohexane-Degrading Bacterium.";
RL   Genome Announc. 1:e00956-13(2013).
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:EQB34026.1}.
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DR   EMBL; AUWY01000022; EQB34026.1; -; Genomic_DNA.
DR   RefSeq; WP_021316354.1; NZ_AUWY01000022.1.
DR   AlphaFoldDB; T0J7T6; -.
DR   STRING; 1346791.M529_01490; -.
DR   PATRIC; fig|1346791.3.peg.285; -.
DR   eggNOG; COG0498; Bacteria.
DR   OrthoDB; 9778118at2; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000015523; 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; cd01563; Thr-synth_1; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
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; PTHR48078:SF6; ACT DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00291; PALP; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015523};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          83..388
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         122
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   414 AA;  44481 MW;  292EA548CA4C48DC CRC64;
     MRHDLNLTID RPTFVTHLEC SLTGERYEAD RLHGLSAAGK PLLVRYDLDG VKAALTKDAL
     AARPMDLWRW RELLPVRHTK NIVSLGEQAT PLIPLPRTAA RIGGSGTLLA KDEGRLPTAS
     FKARGLVMAV SMAKELGVTQ VAMPTNGNAG AALAAYAAVA GMEAIIFCPA DTPEVNVREI
     AAQGARVYRV NGLIDDCGAI VGEGAKQRGW FDFSTLKEPY RIEGKKTMGL ELAEQLGWEL
     PDAIFYPTGG GTGLIGMWKA FDELEKIGFI GSKRPKMFAV QAEGCAPMVR AFEAGEEFAP
     RWENAHTIAS GIRVPRAVGD FLILRAVRES GGAALAVSDE AIAAAVRDVA RDDGLLMCPE
     GGATLAAYQR ALDEGLIARD ARVVLFNCAS GLKYPLEDQS RTLDRHAPID FAAL
//
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