ID M0ZR79_SOLTU Unreviewed; 519 AA.
AC M0ZR79;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=threonine synthase {ECO:0000256|ARBA:ARBA00013028};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN Name=102577745 {ECO:0000313|EnsemblPlants:PGSC0003DMT400006366};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400006366, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400006366}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400006366};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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 -!- 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_006342954.1; XM_006342892.2.
DR AlphaFoldDB; M0ZR79; -.
DR STRING; 4113.M0ZR79; -.
DR EnsemblPlants; PGSC0003DMT400006366; PGSC0003DMT400006366; PGSC0003DMG400002486.
DR GeneID; 102577745; -.
DR Gramene; PGSC0003DMT400006366; PGSC0003DMT400006366; PGSC0003DMG400002486.
DR HOGENOM; CLU_028142_5_0_1; -.
DR InParanoid; M0ZR79; -.
DR OMA; KLEGCNP; -.
DR OrthoDB; 544888at2759; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M0ZR79; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004795; F:threonine synthase activity; IBA:GO_Central.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
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; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF258; THREONINE SYNTHASE, CHLOROPLASTIC; 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:UP000011115};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 158..465
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 196
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 519 AA; 57412 MW; 114C09785BC61464 CRC64;
MAASCMLRSS FLSPGLPQLH HQSTSKPNNG IHFFTPIKAT ATNDAISQQK HRRPADENIR
EEARRHCSSH NFSARYVPFN AGPNSDEWYS LDEIVYRSRS GGLLDVQHDM DALKKFDGQY
WRSLFDSRVG KTTWPYGSGV WSKKEWVLPE IDSDDIVSAF EGNSNLFWAE RFGKQFLGMT
DLWVKHCGIS HTGSFKDLGM TVLVSQVNRL RKMHKPVVGV GCASTGDTSA ALSAYCASAG
IPSIVFLPAN KISMAQLVQP IANGAFVLSI DTDFDGCMQL IREVTAELPI YLANSLNSLR
LEGQKTAAIE ILQQFDWEVP EWVIVPGGNL GNIYAFYKGF QMCKELGLVD RIPRLVCAQA
ANANPLYLHY KSGWKDFKPV KANTTFASAI QIGDPVSIDR AVFALQQCNG IVEEATEEEL
MDAMAQADST GMFICPHTGV ALTALFKLRN SGVIAPTDRT VVVSTAHGLK FTQSKIDYHS
KEIKDMECRF ANPPVEVKAD FGSVMDVLKS YLLSQNSKL
//
