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Database: UniProt
Entry: A0A0L1J9J0_ASPNO
LinkDB: A0A0L1J9J0_ASPNO
Original site: A0A0L1J9J0_ASPNO 
ID   A0A0L1J9J0_ASPNO        Unreviewed;       308 AA.
AC   A0A0L1J9J0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Dihydrodipicolinate synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ANOM_004295 {ECO:0000313|EMBL:KNG88419.1};
OS   Aspergillus nomiae NRRL 13137.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG88419.1, ECO:0000313|Proteomes:UP000037505};
RN   [1] {ECO:0000313|EMBL:KNG88419.1, ECO:0000313|Proteomes:UP000037505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG88419.1,
RC   ECO:0000313|Proteomes:UP000037505};
RA   Moore M.G., Shannon B.M., Brian M.M.;
RT   "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:KNG88419.1}.
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DR   EMBL; JNOM01000053; KNG88419.1; -; Genomic_DNA.
DR   RefSeq; XP_015409342.1; XM_015549552.1.
DR   AlphaFoldDB; A0A0L1J9J0; -.
DR   STRING; 1509407.A0A0L1J9J0; -.
DR   GeneID; 26806099; -.
DR   OrthoDB; 1705410at2759; -.
DR   Proteomes; UP000037505; 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:SF73; 4-HYDROXY-TETRAHYDRODIPICOLINATE SYNTHASE; 1.
DR   PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 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:UP000037505}.
FT   ACT_SITE        139
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        167
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         51
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   308 AA;  33241 MW;  901A2622F51B5B51 CRC64;
     MRNTRNIFEG LVAFPITPTD SHGIVNTATL GRIIERLDIP GVDSIGLLGS TGTYMYLTRA
     QRKRALDAAI QTLQGRKPLI VSVGALRTDD AQQLAKDAEE AGADGLLLAP VSYNPLSEEE
     VYQHYESVTG STTLPLCIYN TPSTTHFTFS DTLLACIAGL PNVVALKQPA PASEATERHE
     ALRAKLPSGF SIGYSADWLV ADSLLAGGSA WYSVIAGVLP APSVALMAAI RKGDDIEVRR
     ISALFQPMWD LFEELSDLKV AFALANELDL CKAAPPRPIL PIAASHHNRI RSALARLNEG
     IKEMPWKI
//
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