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Database: UniProt
Entry: B1L3S1_KORCO
LinkDB: B1L3S1_KORCO
Original site: B1L3S1_KORCO 
ID   B1L3S1_KORCO            Unreviewed;       299 AA.
AC   B1L3S1;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Dihydrodipicolinate synthetase {ECO:0000313|EMBL:ACB07100.1};
GN   OrderedLocusNames=Kcr_0342 {ECO:0000313|EMBL:ACB07100.1};
OS   Korarchaeum cryptofilum (strain OPF8).
OC   Archaea; Candidatus Korarchaeota; Korarchaeum.
OX   NCBI_TaxID=374847 {ECO:0000313|EMBL:ACB07100.1, ECO:0000313|Proteomes:UP000001686};
RN   [1] {ECO:0000313|EMBL:ACB07100.1, ECO:0000313|Proteomes:UP000001686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OPF8 {ECO:0000313|Proteomes:UP000001686};
RX   PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA   Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA   Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA   Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA   Richardson P., Keller M., Stetter K.O.;
RT   "A korarchaeal genome reveals new insights into the evolution of the
RT   Archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008).
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DR   EMBL; CP000968; ACB07100.1; -; Genomic_DNA.
DR   RefSeq; WP_012308997.1; NC_010482.1.
DR   AlphaFoldDB; B1L3S1; -.
DR   STRING; 374847.Kcr_0342; -.
DR   EnsemblBacteria; ACB07100; ACB07100; Kcr_0342.
DR   GeneID; 6093630; -.
DR   KEGG; kcr:Kcr_0342; -.
DR   eggNOG; arCOG04172; Archaea.
DR   HOGENOM; CLU_049343_5_1_2; -.
DR   InParanoid; B1L3S1; -.
DR   OrthoDB; 33636at2157; -.
DR   PhylomeDB; B1L3S1; -.
DR   Proteomes; UP000001686; Chromosome.
DR   GO; GO:0008675; F:2-dehydro-3-deoxy-phosphogluconate aldolase activity; IEA:UniProt.
DR   GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IBA:GO_Central.
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   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001686}.
FT   ACT_SITE        134
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        163
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         46
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT   BINDING         208
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   299 AA;  33055 MW;  C005F26F1C972CAA CRC64;
     MSFRGIITPL ITPFNEKLEI DFDALRWLAN HQLRGGVHGI FPNSTTGEFV HLEREEAIRL
     TEALIDEVGG KIWVIPGISH NSTDKAVELG NIFKDMGADG VIVTPPFFFK IDAKKLGLHF
     SRIADRVDLP IIIYNIPSLT GINVPIELYI ELAQEHSNIA GAKVTYDSFS YLRRLIQGIK
     SVRKDFSVLT GMDDLLLFNL MMGGDGGITA LANLIPSLHR AIYDAWENGD LRRALEENYK
     LLKLSSIYDI ASSFPTAIKT ALNVMGTPVK PHVRPPLTEE PGSVVTAITG VLRELGLHD
//
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