KDSA_PEA
ID KDSA_PEA Reviewed; 290 AA.
AC O50044;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase;
DE EC=2.5.1.55 {ECO:0000250|UniProtKB:Q9AV97};
DE AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase;
DE AltName: Full=KDO-8-phosphate synthase;
DE Short=KDO 8-P synthase;
DE Short=KDOPS;
DE AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase;
GN Name=KDSA;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Die kleine Rheinlaenderin;
RX PubMed=11219578; DOI=10.1007/s004250000459;
RA Brabetz W., Wolter F.P., Brade H.;
RT "A cDNA encoding 3-deoxy-D-manno-oct-2-ulosonate-8-phosphate synthase of
RT Pisum sativum L. (pea) functionally complements a kdsA mutant of the Gram-
RT negative bacterium Salmonella enterica.";
RL Planta 212:136-143(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 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:0000250|UniProtKB:Q9AV97};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000305}.
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DR EMBL; Y14273; CAA74645.1; -; mRNA.
DR EMBL; Y14272; CAA74644.1; -; mRNA.
DR PIR; T06816; T06816.
DR AlphaFoldDB; O50044; -.
DR SMR; O50044; -.
DR EnsemblPlants; Psat3g099560.1; Psat3g099560.1.cds; Psat3g099560.
DR Gramene; Psat3g099560.1; Psat3g099560.1.cds; Psat3g099560.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008676; F:3-deoxy-8-phosphooctulonate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00056; KDO8P_synth; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR006269; KDO8P_synthase.
DR PANTHER; PTHR21057; PTHR21057; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR TIGRFAMs; TIGR01362; KDO8P_synth; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Transferase.
FT CHAIN 1..290
FT /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT /id="PRO_0000187180"
SQ SEQUENCE 290 AA; 31723 MW; 56F37C3779FBF398 CRC64;
MDPSVLLYNQ LKAADPFFLL AGPNVIESEE HIMRMAKHIK TISSKFGIPL IFKSSFDKAN
RTSSKSFRGP GIVEGLKILE KVKIAYDIPI VTDVHEASQC EPVGRVADII QIPAFLCRQT
DLLVAAAKTG KIINIKKGQF CAPSVMANSA EKVRLAGNPN VMVCERGTMF GYNDLIVDPR
NLEWMREANC PVVADITHSL QQPAGKKLDG GGVASGGLRE LIPCIARTSV AVGVDGIFME
VHDDPLNAPV DGPTQWPLRH LEELLEELIA ISRVSKGKKP FNIDLTPFRE