GenomeNet

Database: UniProt
Entry: A0A2J6KBZ5_LACSA
LinkDB: A0A2J6KBZ5_LACSA
Original site: A0A2J6KBZ5_LACSA 
ID   A0A2J6KBZ5_LACSA        Unreviewed;       523 AA.
AC   A0A2J6KBZ5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=threonine synthase {ECO:0000256|ARBA:ARBA00013028};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   ORFNames=LSAT_5X21680 {ECO:0000313|EMBL:PLY72605.1};
OS   Lactuca sativa (Garden lettuce).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC   Lactucinae; Lactuca.
OX   NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY72605.1};
RN   [1] {ECO:0000313|EMBL:PLY72605.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28401891; DOI=10.1038/ncomms14953;
RA   Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA   Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA   Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT   "Genome assembly with in vitro proximity ligation data and whole-genome
RT   triplication in lettuce.";
RL   Nat. Commun. 8:14953-14953(2017).
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:PLY72605.1}.
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   EMBL; NBSK01007972; PLY72605.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6KBZ5; -.
DR   STRING; 4236.A0A2J6KBZ5; -.
DR   EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_5X21680_mrna; cds-PLY72605.1; gene-LSAT_5X21680.
DR   Gramene; rna-gnl|WGS:NBSK|LSAT_5X21680_mrna; cds-PLY72605.1; gene-LSAT_5X21680.
DR   OrthoDB; 544888at2759; -.
DR   UniPathway; UPA00050; UER00065.
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:SF5; THREONINE SYNTHASE 2, 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   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          162..469
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         200
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   523 AA;  57594 MW;  665FDDA68F51ED93 CRC64;
     MAASSLLRSS PFFSSPQQRN PRTINKSPRF ITIKATISSS DKSVDTTPVI KSHRRPADEN
     IRQEAHRRCS TEPNNFSAKY VPFNADPGCT ESYSLDEIVY RSRSGGLLDV QHDMEALKEF
     DGNYWKNLFD GRIGKTNWPY GSGVWSKKEW VLPEIDSDDI VSAFEGNSNM FWAERYGKQH
     LGMNDLWVKH CGISHTGSFK DLGMTVLVSQ VNRLRKMNRP VVGVGCASTG DTSAALSAYC
     ASAGIPSIVF LPANKISMAQ LVQPIANGAF VLSLDTDFDG CMQLVREVTS ELPIYLANSL
     NSLRIEGQKT AAIEILQQFD WEVPDWVIVP GGNLGNIYAF YKGFQMCKEL GLVDRIPRLV
     CAQAANANPL YLHYKSGWTD FSPVKAKTTF ASAIQIGDPV SIDRAVYALQ NSNGIVEEAT
     EEELMDAMAQ ADSTGMFICP HTGVALTALD KLRNSGVIRP TDRTVVVSTA HGLKFTQSKI
     DYHSKAIPEM ACSLANPPVN VKADFGSVMD VLKKYLLSKE SKN
//
DBGET integrated database retrieval system