ID A0A395RYS1_FUSSP Unreviewed; 345 AA.
AC A0A395RYS1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 10.
DE SubName: Full=Dihydrodipicolinate synthase {ECO:0000313|EMBL:RGP65251.1};
GN ORFNames=FSPOR_7385 {ECO:0000313|EMBL:RGP65251.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP65251.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP65251.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP65251.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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:RGP65251.1}.
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; PXOF01000105; RGP65251.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395RYS1; -.
DR STRING; 5514.A0A395RYS1; -.
DR Proteomes; UP000266152; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR CDD; cd00408; DHDPS-like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR PANTHER; PTHR12128:SF47; DIHYDRODIPICOLINATE SYNTHETASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_2G01230); 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000266152}.
FT ACT_SITE 142
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 172
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 215
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 345 AA; 36505 MW; E010DF7750A54542 CRC64;
MSPRTAPPSG VWAPAITFFD HDTDTLDTDS QAAYYSYLSK TGLAGLVVLG TNAETFMLTR
EERKELLQTA RRACGPDFPI MAGVGGHSTK QVLEFISDAS DAGANYVLLL PPAYFGKQTT
PEVINNFFDD VATKSQLPIV IYNFPVVCNG IDLDSATIAA LAKKHSNIVG VKLTCGAVAK
ITRLAAELPE ERFSIYGGQS DFLIGGLAAG SHGTIAGFAN VVPKTIVHIY NLYQEGKFQE
AMALHKKAAL AEQPCKAGIA SVKYAATLST AKAAGIKGAA DKLKPRRPYV EPSNTAKESI
QAQIAEMLSF EATLKPAVEN GHTNGIAKEV ANGVTNGACN GVEVH
//
