ID M0MI08_9EURY Unreviewed; 300 AA.
AC M0MI08;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Dihydrodipicolinate synthase {ECO:0000313|EMBL:EMA44973.1};
GN ORFNames=C449_09959 {ECO:0000313|EMBL:EMA44973.1};
OS Halococcus saccharolyticus DSM 5350.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halococcus.
OX NCBI_TaxID=1227455 {ECO:0000313|EMBL:EMA44973.1, ECO:0000313|Proteomes:UP000011669};
RN [1] {ECO:0000313|EMBL:EMA44973.1, ECO:0000313|Proteomes:UP000011669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5350 {ECO:0000313|EMBL:EMA44973.1,
RC ECO:0000313|Proteomes:UP000011669};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|ARBA:ARBA00007592}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMA44973.1}.
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DR EMBL; AOMD01000021; EMA44973.1; -; Genomic_DNA.
DR RefSeq; WP_006077843.1; NZ_AOMD01000021.1.
DR AlphaFoldDB; M0MI08; -.
DR STRING; 1227455.C449_09959; -.
DR PATRIC; fig|1227455.4.peg.2039; -.
DR InParanoid; M0MI08; -.
DR OrthoDB; 350860at2157; -.
DR Proteomes; UP000011669; Unassembled WGS sequence.
DR GO; GO:0008675; F:2-dehydro-3-deoxy-phosphogluconate aldolase activity; IEA:UniProt.
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 InterPro; IPR020625; Schiff_base-form_aldolases_AS.
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.
DR PROSITE; PS00666; DHDPS_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000011669};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT ACT_SITE 143
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 212
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 300 AA; 31687 MW; 1BA3D884A981C87A CRC64;
MQSDSNPDPL SSGGVIPPTV TAFHGDESVD YGTTAAHARF VVDRGVDGVF PLGTNGEFAL
LDAEESVGVI EAVVDEVGGE VPVIAGVGAV STYHTVRNAE RAADAGADGV MIVTPYYYPL
DDEGAIEHYQ RVADAIDLPI YVYHIPGRTG NELSRGTLAE LAEIDAIAGI KDSSKDVPWL
GQTIATNPDL TVLPGADSLQ FVGRVLGGVG GVSAIANAFP EIVVDLHDAY DAGDRDRARD
LQETLYRIRA AFDKGPYMAG VKGALSLQGF DAGPLRSPLR RLTDEQKNEL ERDLQGLGVL
//
