ID A0A0P7GB18_9EURY Unreviewed; 303 AA.
AC A0A0P7GB18;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000313|EMBL:KPN30702.1};
DE EC=4.3.3.7 {ECO:0000313|EMBL:KPN30702.1};
GN Name=dapA_1 {ECO:0000313|EMBL:KPN30702.1};
GN ORFNames=SY89_01438 {ECO:0000313|EMBL:KPN30702.1};
OS Halolamina pelagica.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae.
OX NCBI_TaxID=699431 {ECO:0000313|EMBL:KPN30702.1, ECO:0000313|Proteomes:UP000050535};
RN [1] {ECO:0000313|Proteomes:UP000050535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDK2 {ECO:0000313|Proteomes:UP000050535};
RA Hoang H.T., Killian M.L., Madson D.M., Arruda P.H.E., Sun D.,
RA Schwartz K.J., Yoon K.;
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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:KPN30702.1}.
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DR EMBL; LGUC01000001; KPN30702.1; -; Genomic_DNA.
DR RefSeq; WP_054583588.1; NZ_LGUC01000001.1.
DR AlphaFoldDB; A0A0P7GB18; -.
DR STRING; 699431.SY89_01438; -.
DR PATRIC; fig|699431.3.peg.1471; -.
DR OrthoDB; 33636at2157; -.
DR Proteomes; UP000050535; Unassembled WGS sequence.
DR GO; GO:0008675; F:2-dehydro-3-deoxy-phosphogluconate aldolase activity; IEA:UniProt.
DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-EC.
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 Lyase {ECO:0000313|EMBL:KPN30702.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050535};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT ACT_SITE 145
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 173
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 214
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 303 AA; 31992 MW; 5A19751DF31CDF1A CRC64;
MAAPDPGAAD PLSLHGVVPP TVTAFDDDGA LDAETTAEHA RFVVDRGVHG VFPLGTNGEF
ALLGPEERDE VVRAVVEEVG EEVPVIAGVG EPATRRTVER AQAAERAGAD GVVVVTPYYY
PLDGAAAVEH YRTVCAAVDC PVYVYHIPSK TGNELSLETL EEIAAIDNLA GLKDSSKDVP
WLGQAVAAHD DLTFLAGSDS LLKPGLDLGC TGMVSAVANA FPELVVDLYE AYDAGDRERA
TTLQAQVYEV RSAIKRGPYM AGVKEALSHR GFDAGPLRSP LRRMDDADSA ALREELAALG
LLE
//
