ID   A0A178EFC0_9PLEO        Unreviewed;       313 AA.
AC   A0A178EFC0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Dihydrodipicolinate synthetase family protein-like protein {ECO:0000313|EMBL:OAL54707.1};
GN   ORFNames=IQ07DRAFT_583919 {ECO:0000313|EMBL:OAL54707.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL54707.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL54707.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL54707.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DapA family.
CC       {ECO:0000256|PIRNR:PIRNR001365}.
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DR   EMBL; KV441638; OAL54707.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178EFC0; -.
DR   STRING; 765867.A0A178EFC0; -.
DR   InParanoid; A0A178EFC0; -.
DR   OrthoDB; 1780992at2759; -.
DR   Proteomes; UP000077535; 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   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:UP000077535}.
FT   ACT_SITE        140
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        171
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         214
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   313 AA;  33316 MW;  1CF1EAAA6225E82A CRC64;
     MASLPAPGVW CPSVTFFDST TSHLDIAAQK QYFSYLSKSG LAGLVVLGSN QEAFLLTREE
     RIALIKAARE AVGPDYPLMV GVSSFSVPQV LENIQDAIKA GANYGLLLPA AYYGPQTTKE
     VVKGFYNEVA QKSDLPLVIY NFPGISNGVD LDSVTIAELA KSNPGKIVGV KLTCGSVAKI
     TRLCAELPSE TFSVYAGQAD WLIAGLAVGA VGCVSAFSNV FPKTLSKIYD LYVSGNTKEA
     LELHRKAALA ESPVKAGIAA VKHAVSQYTA KAAGIENPEE KLNPRRPYLP VGAAVQTNIK
     SAMDELWEIE KSI
//