ID A0A3M6VJG4_9STRA Unreviewed; 532 AA.
AC A0A3M6VJG4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Threonine synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=DD238_000963 {ECO:0000313|EMBL:RMX66904.1};
OS Peronospora effusa.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Peronospora.
OX NCBI_TaxID=542832 {ECO:0000313|EMBL:RMX66904.1, ECO:0000313|Proteomes:UP000282087};
RN [1] {ECO:0000313|EMBL:RMX66904.1, ECO:0000313|Proteomes:UP000282087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R14 {ECO:0000313|EMBL:RMX66904.1,
RC ECO:0000313|Proteomes:UP000282087};
RA Fletcher K., Klosterman S.J., Derevnina L., Martin F., Koike S.,
RA Reyes Chin-Wo S., Mou B., Michelmore R.;
RT "Comparative genomics of downy mildews reveals potential adaptations to
RT biotrophy.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR604450-51};
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:RMX66904.1}.
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DR EMBL; QLLG01000183; RMX66904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M6VJG4; -.
DR STRING; 542832.A0A3M6VJG4; -.
DR VEuPathDB; FungiDB:DD237_001724; -.
DR Proteomes; UP000282087; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239}; Membrane {ECO:0000256|SAM:Phobius};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000282087};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 511..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..84
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 105..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 532 AA; 58369 MW; 46AC73ECBE6D979D CRC64;
MVHYRSTRGG VRGLSFEQAV LTGLASDRGL LVPEANEFPT LPTGALDKWA SLSYQELAVE
VMGLFIDESE ISRDELRSLV DKSYNLTTFR AKEVAPVVKV SDHMLVLELF HGPTFAFKDI
ALQFLGNLFE FFLQRKNAVL PDGAPQYQIT VVGATSGDTG SSAIYGLRGK KNVEVFILFP
EGRVSAIQQR QMTTVLDENI HNVAVKGTFD DCQAIVKDLF ANAEFKAKYH LGAVNSINFA
RILAQVVYYV WAYFRAREQG VSGEVAFSVP TGNFGDILAG FYAKKLGVPI GKLIVATNEN
DILHRFFCKG KYHRHDIKHT ITPSMDICVS SNFERYLFAL SGENHDILRD WMQGFEQTGE
LTISGELLAK AQDEMASYAV LQEEVRSTIA QYSKVQHYLF DPHSAIGAAA AMRFGMDALA
DKPGLAVVVV GTAHYGKFLP VVSKALGVTE AEIEQHPILK ALESLSTRLA TANNSSATVA
EYIRKTIGKK NQKACGEGGQ MWASIPKESK LVSLALAAAA VAVAFFVTRR SK
//
