ID A0A165ETZ6_9APHY Unreviewed; 310 AA.
AC A0A165ETZ6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Dihydrodipicolinate synthetase {ECO:0000313|EMBL:KZT07757.1};
GN ORFNames=LAESUDRAFT_736334 {ECO:0000313|EMBL:KZT07757.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT07757.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT07757.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT07757.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; KV427618; KZT07757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165ETZ6; -.
DR STRING; 1314785.A0A165ETZ6; -.
DR InParanoid; A0A165ETZ6; -.
DR OrthoDB; 1780992at2759; -.
DR Proteomes; UP000076871; 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:SF72; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL; 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:UP000076871}.
FT ACT_SITE 147
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 176
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 219
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 310 AA; 32756 MW; CD7652D7E375237D CRC64;
MAPVNSTPPP PGVYVPAVLF FDENEEFDVP AIKAHILRLA KGGVTGILVQ GSNGEAQHLS
HDERKEAIRL TRQTLNENGF QDVVIVAGTG AQSTRETKKL CADAAEAGAA YCLVLTPSVW
PAQMTAEKIF KFHRDVADAS PIPTMIYNFP VVTAGLNLDS DIIGALAQHP NIVGTKLSCG
MVGKLHRLTS SVPASKFATF PGVSDVFLQG LVSGSAGLIG ALPNVAPKAH MEVYRLYKAG
KLEEATKIQA LLGHADWELG KLGSIGGIKA VVSKHFGYGT TVVRGPLSAA VITTANTQKL
DELIVLEKSL
//
