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Database: UniProt
Entry: A0A8K0JBQ2_9HYPO
LinkDB: A0A8K0JBQ2_9HYPO
Original site: A0A8K0JBQ2_9HYPO 
ID   A0A8K0JBQ2_9HYPO        Unreviewed;       315 AA.
AC   A0A8K0JBQ2;
DT   03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT   03-AUG-2022, sequence version 1.
DT   05-FEB-2025, entry version 10.
DE   SubName: Full=L-threo-3-deoxy-hexylosonate aldolase {ECO:0000313|EMBL:KAG5927952.1};
GN   Name=LGA1 {ECO:0000313|EMBL:KAG5927952.1};
GN   ORFNames=E4U42_001489 {ECO:0000313|EMBL:KAG5927952.1};
OS   Claviceps africana.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=83212 {ECO:0000313|EMBL:KAG5927952.1, ECO:0000313|Proteomes:UP000811619};
RN   [1] {ECO:0000313|EMBL:KAG5927952.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCC 489 {ECO:0000313|EMBL:KAG5927952.1};
RA   Wyka S.A., Mondo S.J., Liu M., Dettman J., Nalam V., Broders K.D.;
RT   "Whole genome comparisons of ergot fungi reveals the divergence and
RT   evolution of species within the genus Claviceps are the result of varying
RT   mechanisms driving genome evolution and host range expansion.";
RL   bioRxiv 0:0-0(2020).
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:KAG5927952.1}.
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DR   EMBL; SRPY01000145; KAG5927952.1; -; Genomic_DNA.
DR   OrthoDB; 191315at2759; -.
DR   Proteomes; UP000811619; Unassembled WGS sequence.
DR   GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:TreeGrafter.
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:SF24; DIHYDRODIPICOLINATE SYNTHETASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_3G11920); 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:UP000811619}.
FT   ACT_SITE        145
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        174
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         224
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   315 AA;  33533 MW;  55ACAB537D4FDA7D CRC64;
     MARRALPCGI YAPTPTFFDA ETEDLDMPTI KKHAQRLVRD GLVGLVVMGS NGEAVHCTRD
     EKIAVTRATR EALDDAGFAS TPIILGATEG SVRGTLELTR LAADAGADYT LLLPPSYYRA
     QIDDESIVQY FTDVADASPL PVIVYNYPGA VSGIDLDSDV LLSLGQHPNI VGTKFTCGNT
     GKLTRVALGT HAKTPFQEGS GYMAFGGMCD FTMQTVASGG SGIIAGGANL MPKVCVRVWD
     LYAEGKKDEA AALQKILSRA DWHLTKTAIA GTKLAIEAHH GYGGYPRRPL KRLDGPKMKA
     LLEGVEQAMS VEGSL
//
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