GenomeNet

Database: UniProt
Entry: A0A067BY40_SAPPC
LinkDB: A0A067BY40_SAPPC
Original site: A0A067BY40_SAPPC 
ID   A0A067BY40_SAPPC        Unreviewed;       529 AA.
AC   A0A067BY40;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=threonine synthase {ECO:0000256|ARBA:ARBA00013028};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   ORFNames=SPRG_15659 {ECO:0000313|EMBL:KDO19216.1};
OS   Saprolegnia parasitica (strain CBS 223.65).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Saprolegnia.
OX   NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO19216.1, ECO:0000313|Proteomes:UP000030745};
RN   [1] {ECO:0000313|EMBL:KDO19216.1, ECO:0000313|Proteomes:UP000030745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO19216.1,
RC   ECO:0000313|Proteomes:UP000030745};
RX   PubMed=23785293;
RA   Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA   van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA   Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA   Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA   Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA   Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA   Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA   Russ C., Tyler B.M., van West P.;
RT   "Distinctive expansion of potential virulence genes in the genome of the
RT   oomycete fish pathogen Saprolegnia parasitica.";
RL   PLoS Genet. 9:E1003272-E1003272(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   ---------------------------------------------------------------------------
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; KK583364; KDO19216.1; -; Genomic_DNA.
DR   RefSeq; XP_012210082.1; XM_012354692.1.
DR   AlphaFoldDB; A0A067BY40; -.
DR   STRING; 695850.A0A067BY40; -.
DR   EnsemblProtists; KDO19216; KDO19216; SPRG_15659.
DR   GeneID; 24137367; -.
DR   KEGG; spar:SPRG_15659; -.
DR   VEuPathDB; FungiDB:SPRG_15659; -.
DR   OMA; FNRCQHL; -.
DR   OrthoDB; 275600at2759; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000030745; 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   Reference proteome {ECO:0000313|Proteomes:UP000030745};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          3..82
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          104..341
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         118
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   529 AA;  57959 MW;  EE4CAFBB87D40219 CRC64;
     MTKYQSTRGG VRGFSFEEAV LSGLAADRGL FVPESIPQLP EGALEAWAKL SYEELAVEVM
     SLFIDDAEIP RADLTELVAK AYTCSETNFR DPTIAPIVQV KDQLYMLELF HGPTFAFKDV
     ALQFLGHLFE YFLERKNRNE TSGKTHRITV VGATSGDTGS AAIYGLRNKK NVEVFIMYPH
     GRVSAIQEQQ MACILDENIH NLAVKGTFDD CQAIVKDCFA DAEFKAAYSL GAVNSINWAR
     ILAQIVYYFY AYFRLSPEAQ KKVAFSVPTG NFGDILAGFY AMKLGLPMQK LIVATNDNDI
     LHRFFSTGAY HRSGVSHTIS PSMDICVSSN FERYLFSLCG DDAAVLHQWM STFEATGKLT
     VEGPLLAKAK HEMASYSVLE PEVLQTIQTY HDAHNYVLDP HSAIGVAAGD AYLRDMADPD
     VTVVVLATAH YGKFMPTVQS AFSTPVALPQ HPILKALESL PQKSHVTENS VAAVQALVRE
     TVPVAKKQMP CCVFGAASYL LPESNALKAA LVIAVGAVAV VALQRSTKH
//
DBGET integrated database retrieval system