ID A0A0D2CH91_9EURO Unreviewed; 319 AA.
AC A0A0D2CH91;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Dihydrodipicolinate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV07_11190 {ECO:0000313|EMBL:KIW22949.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW22949.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW22949.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW22949.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; KN847046; KIW22949.1; -; Genomic_DNA.
DR RefSeq; XP_016243165.1; XM_016398603.1.
DR AlphaFoldDB; A0A0D2CH91; -.
DR STRING; 569365.A0A0D2CH91; -.
DR GeneID; 27350384; -.
DR VEuPathDB; FungiDB:PV07_11190; -.
DR HOGENOM; CLU_049343_0_2_1; -.
DR OrthoDB; 1780992at2759; -.
DR Proteomes; UP000054466; 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:SF52; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL-RELATED; 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:UP000054466}.
FT ACT_SITE 149
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 178
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 228
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 319 AA; 33967 MW; 6EC7769BE3750B46 CRC64;
MNGHHTARPL RPGINVPMVT IFDPETEDVD VKAIAKHAVR LAQAGLSSIT CQGSNGEAVH
LTKEERILVT STTRKALDEA GFSDMPIVVG CGAQSVRETI EFCRDAYQAG GDCALVLPPS
YYKSAYKPES FVEYFQAVAD GSPIPIVIYN YPGAVAGVDL DSDTIIKLAK HPNIRGCKLT
CGNTGKLNRI AHAVNAATPN DLGSGWMCMG GSADFTLQTL IAGGSGIITG LGNVVPKACV
KVYDLYAQGK VEEAQKLQAI VARGDWGVIA GGITGTKSAM QSYFGYGGYA RRPLPKPTKE
EVAKWEEMLK EAVELENSL
//
