ID M7XEK4_RHOT1 Unreviewed; 318 AA.
AC M7XEK4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Dihydrodipicolinate synthase {ECO:0000313|EMBL:EMS18568.1};
GN ORFNames=RHTO_05820 {ECO:0000313|EMBL:EMS18568.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS18568.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS18568.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS18568.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; KB722678; EMS18568.1; -; Genomic_DNA.
DR RefSeq; XP_016269687.1; XM_016419481.1.
DR AlphaFoldDB; M7XEK4; -.
DR GeneID; 27369833; -.
DR eggNOG; ENOG502QWNS; Eukaryota.
DR HOGENOM; CLU_049343_0_2_1; -.
DR OrthoDB; 1780992at2759; -.
DR Proteomes; UP000016926; 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}.
FT ACT_SITE 149
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 179
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 220
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 318 AA; 33412 MW; 2FEB779C8C9C1839 CRC64;
MPSTKFGKNL PHGVYAPVLT FYKGNDEELD LETYKKHVQF VARGGVNIVA LGSMGESVQL
THQERNQVVK AARSALDADS SLSQVPLIAG TGASSTKETI ELTKEAAEAG ADFAMVISPG
YFAGAMSRKA IKQFFVDVAE ASPIPVLVYN YPGASAGIDI DSDLMAEIAA AAPNIVGCKL
TCGSVGKLTR LTTLRDDFAV LGGFIDFLGP SLLAKAAGGI TGVGNVAPKT CAKLYKDTLA
ALSGQASVSS AQDLQFIVSR ADWALAKTGI AGAKWVLDQL EGYGGKPRRP LLPFDESDGK
GKQLLDDLKE ILEVEKSL
//
