ID   A7TDC1_NEMVE            Unreviewed;       246 AA.
AC   A7TDC1;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   04-NOV-2026, entry version 74.
DE   RecName: Full=3-deoxy-8-phosphooctulonate synthase {ECO:0000256|ARBA:ARBA00012693};
DE            EC=2.5.1.55 {ECO:0000256|ARBA:ARBA00012693};
DE   Flags: Fragment;
GN   ORFNames=NEMVEDRAFT_v1g155958 {ECO:0000313|EMBL:EDO25931.1};
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO25931.1, ECO:0000313|Proteomes:UP000001593};
RN   [1] {ECO:0000313|EMBL:EDO25931.1, ECO:0000313|Proteomes:UP000001593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-arabinose 5-phosphate + phosphoenolpyruvate + H2O = 3-deoxy-
CC         alpha-D-manno-2-octulosonate-8-phosphate + phosphate;
CC         Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;
CC         Evidence={ECO:0000256|ARBA:ARBA00049112};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PROSITE-ProRule:PRU01406}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01406}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01406}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS477579; EDO25931.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7TDC1; -.
DR   STRING; 45351.A7TDC1; -.
DR   KEGG; nve:5496248; -.
DR   eggNOG; ENOG502QQN7; Eukaryota.
DR   HOGENOM; CLU_036666_0_0_1; -.
DR   InParanoid; A7TDC1; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008676; F:3-deoxy-8-phosphooctulonate synthase activity; IBA:GO_Central.
DR   GO; GO:0046364; P:monosaccharide biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006269; KDO8P_synthase.
DR   NCBIfam; TIGR01362; KDO8P_synth; 1.
DR   NCBIfam; NF003543; kdsA; 1.
DR   PANTHER; PTHR21057; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS52061; DAHPS_I; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PROSITE-
KW   ProRule:PRU01406}; Reference proteome {ECO:0000313|Proteomes:UP000001593};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01406}.
FT   DOMAIN          14..246
FT                   /note="DAHPS class-I TIM-barrel"
FT                   /evidence="ECO:0000259|PROSITE:PS52061"
FT   BINDING         24
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
FT   BINDING         53
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
FT   BINDING         58
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
FT   BINDING         136
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
FT   BINDING         166
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
FT   BINDING         197
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
FT   BINDING         234
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
FT   BINDING         245
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01406"
FT   NON_TER         246
FT                   /evidence="ECO:0000313|EMBL:EDO25931.1"
SQ   SEQUENCE   246 AA;  26904 MW;  4BBF54948B4ED521 CRC64;
     MNLDNIPQIK HTKSGNFFLL SGPCAIEGEE MAMRIAEKIV TITDKLEIPY VFKGSFKKAN
     RSRIDSFTGI GDEKALKILA KVAKEFGVPT VTDIHTNEDA VMAAEYVDIL QIPAFLVRQT
     DLVMAAANTG KTVNLKKGQF MSPESMKHAV QKVIDCQNEN VMVTDRGTMF GYQDMIVDYR
     GIPTMQEYAT TVLDVTHSLQ QPNQTVGVTG GRPDMIETVA KAGIAVGVDG IFIETHFDPA
     NAKSDG
//