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Database: UniProt
Entry: B9XMN3_PEDPL
LinkDB: B9XMN3_PEDPL
Original site: B9XMN3_PEDPL 
ID   B9XMN3_PEDPL            Unreviewed;       274 AA.
AC   B9XMN3;
DT   14-APR-2009, integrated into UniProtKB/TrEMBL.
DT   14-APR-2009, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000256|HAMAP-Rule:MF_00056};
DE            EC=2.5.1.55 {ECO:0000256|HAMAP-Rule:MF_00056};
DE   AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE   AltName: Full=KDO-8-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE            Short=KDO 8-P synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE            Short=KDOPS {ECO:0000256|HAMAP-Rule:MF_00056};
DE   AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase {ECO:0000256|HAMAP-Rule:MF_00056};
GN   Name=kdsA {ECO:0000256|HAMAP-Rule:MF_00056};
GN   ORFNames=Cflav_PD2934 {ECO:0000313|EMBL:EEF58932.1};
OS   Pedosphaera parvula (strain Ellin514).
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX   NCBI_TaxID=320771 {ECO:0000313|EMBL:EEF58932.1, ECO:0000313|Proteomes:UP000003688};
RN   [1] {ECO:0000313|EMBL:EEF58932.1, ECO:0000313|Proteomes:UP000003688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin514 {ECO:0000313|EMBL:EEF58932.1,
RC   ECO:0000313|Proteomes:UP000003688};
RX   PubMed=21460084; DOI=10.1128/JB.00299-11;
RA   Kant R., van Passel M.W., Sangwan P., Palva A., Lucas S., Copeland A.,
RA   Lapidus A., Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Larimer F.W., Land M.L., Hauser L., Brettin T.S.,
RA   Detter J.C., Han S., de Vos W.M., Janssen P.H., Smidt H.;
RT   "Genome sequence of 'Pedosphaera parvula' Ellin514, an aerobic
RT   Verrucomicrobial isolate from pasture soil.";
RL   J. Bacteriol. 193:2900-2901(2011).
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:0000256|ARBA:ARBA00001069, ECO:0000256|HAMAP-
CC         Rule:MF_00056};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004756}.
CC   -!- PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate
CC       biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate:
CC       step 2/3. {ECO:0000256|ARBA:ARBA00004845, ECO:0000256|HAMAP-
CC       Rule:MF_00056}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00056}.
CC   -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000256|ARBA:ARBA00010499,
CC       ECO:0000256|HAMAP-Rule:MF_00056}.
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:EEF58932.1}.
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DR   EMBL; ABOX02000035; EEF58932.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9XMN3; -.
DR   STRING; 320771.Cflav_PD2934; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000003688; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008676; F:3-deoxy-8-phosphooctulonate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00056; KDO8P_synth; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006269; KDO8P_synthase.
DR   NCBIfam; TIGR01362; KDO8P_synth; 1.
DR   PANTHER; PTHR21057:SF2; 2-DEHYDRO-3-DEOXYPHOSPHOOCTONATE ALDOLASE 1-RELATED; 1.
DR   PANTHER; PTHR21057; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00056};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00056};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003688};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00056}.
FT   DOMAIN          15..267
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   274 AA;  29393 MW;  DB78B127B55BE73F CRC64;
     MLNDSAIWKS LNSPSRLSLI AGPCAIENEK LCLRIAASLK KTCDKLGINY IFKASYDKAN
     RTSNQSFRGL GLENGLQILA RVRTDIGVPV LTDVHTEQQV AAAAEVVDAL QIPAFLCRQT
     DLIAAAAKTG KIVNVKKGQF LSPQEMGNVV KKAEAAGTKK ICVTERGTTF GYNNLVADMR
     SIPIMSRFGY PVIFDATHSV QLPGGGGDKS SGQREFAPVL ARCALIAGAN GVFIETHPDP
     EHALSDGPNM IPLAEMPRLL ANLVKVHTLA REAK
//
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