ID C1CYB0_DEIDV Unreviewed; 346 AA.
AC C1CYB0;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679, ECO:0000256|PIRNR:PIRNR038945};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028, ECO:0000256|PIRNR:PIRNR038945};
GN OrderedLocusNames=Deide_01270 {ECO:0000313|EMBL:ACO44931.1};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO44931.1, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO44931.1, ECO:0000313|Proteomes:UP000002208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC {ECO:0000313|Proteomes:UP000002208};
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
CC -!- FUNCTION: Catalyzes the gamma-elimination of phosphate from L-
CC phosphohomoserine and the beta-addition of water to produce L-
CC threonine. {ECO:0000256|ARBA:ARBA00003648,
CC ECO:0000256|PIRNR:PIRNR038945}.
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 ECO:0000256|PIRNR:PIRNR038945};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRNR:PIRNR038945, ECO:0000256|PIRSR:PIRSR038945-1};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 5/5. {ECO:0000256|ARBA:ARBA00004979,
CC ECO:0000256|PIRNR:PIRNR038945}.
CC -!- SIMILARITY: Belongs to the threonine synthase family.
CC {ECO:0000256|ARBA:ARBA00005517, ECO:0000256|PIRNR:PIRNR038945}.
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DR EMBL; CP001114; ACO44931.1; -; Genomic_DNA.
DR RefSeq; WP_012692054.1; NC_012526.1.
DR AlphaFoldDB; C1CYB0; -.
DR STRING; 546414.Deide_01270; -.
DR PaxDb; 546414-Deide_01270; -.
DR KEGG; ddr:Deide_01270; -.
DR eggNOG; COG0498; Bacteria.
DR HOGENOM; CLU_028142_0_0_0; -.
DR OrthoDB; 9778118at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000002208; 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 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; IPR026260; Thr_Synthase_bac/arc.
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 PIRSF; PIRSF038945; Thr_synthase; 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 ECO:0000256|PIRNR:PIRNR038945}; Lyase {ECO:0000256|PIRNR:PIRNR038945};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRNR:PIRNR038945};
KW Reference proteome {ECO:0000313|Proteomes:UP000002208};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697,
KW ECO:0000256|PIRNR:PIRNR038945}.
FT DOMAIN 22..315
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT BINDING 84
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT BINDING 184..188
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT BINDING 314
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT MOD_RES 58
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-2"
SQ SEQUENCE 346 AA; 36374 MW; 70140E2C2F1BF2F6 CRC64;
MPGLLERYRS YLPVTDRTPL LSLSEGSTPL IYAPHLSQQL GCELYLKYEG LNPTGSFKDR
GMVMAVAKAM EDGADTVICA STGNTSAAAA AYATRAGLRC IVLIPDGNIA LGKLAQAMAY
GARIVAINGN FDVALNLVRD ISASHPIALV NSVNPYRLQG QKTAAFEIVD ELGSAPDILA
IPVGNAGNIS AYWMGFREYR SAGRMEALPR MYGFQAAGAA PLARGVDRVE NPETLATAIR
IGAPASAHLA RAAVSESGGL FDMVTDDEIM EAQQLVAREG VFCEPASAAP VAGLLKRHAA
GQLPAGQRIV AVLTGNGLKD PNSAMRHVAT PVAVEAQMDR VLESIL
//
