KDSA_AZOSB
ID KDSA_AZOSB Reviewed; 279 AA.
AC A1K7F7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000255|HAMAP-Rule:MF_00056};
DE EC=2.5.1.55 {ECO:0000255|HAMAP-Rule:MF_00056};
DE AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00056};
DE AltName: Full=KDO-8-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00056};
DE Short=KDO 8-P synthase {ECO:0000255|HAMAP-Rule:MF_00056};
DE Short=KDOPS {ECO:0000255|HAMAP-Rule:MF_00056};
DE AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase {ECO:0000255|HAMAP-Rule:MF_00056};
GN Name=kdsA {ECO:0000255|HAMAP-Rule:MF_00056}; OrderedLocusNames=azo2145;
OS Azoarcus sp. (strain BH72).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=418699;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH72;
RX PubMed=17057704; DOI=10.1038/nbt1243;
RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT strain BH72.";
RL Nat. Biotechnol. 24:1385-1391(2006).
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:0000255|HAMAP-Rule:MF_00056};
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:0000255|HAMAP-Rule:MF_00056}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00056}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00056}.
CC -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000255|HAMAP-
CC Rule:MF_00056}.
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DR EMBL; AM406670; CAL94762.1; -; Genomic_DNA.
DR RefSeq; WP_011765876.1; NC_008702.1.
DR AlphaFoldDB; A1K7F7; -.
DR SMR; A1K7F7; -.
DR STRING; 62928.azo2145; -.
DR EnsemblBacteria; CAL94762; CAL94762; azo2145.
DR KEGG; azo:azo2145; -.
DR eggNOG; COG2877; Bacteria.
DR HOGENOM; CLU_036666_0_0_4; -.
DR OMA; FRGIPTM; -.
DR OrthoDB; 687380at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR Proteomes; UP000002588; Chromosome.
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; -; 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 3: Inferred from homology;
KW Cytoplasm; Lipopolysaccharide biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..279
FT /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT /id="PRO_0000304430"
SQ SEQUENCE 279 AA; 29606 MW; BE236BB28FD9066B CRC64;
MNLCGFEVGL DKPVFLIAGP CVIESREMAF ETAGALKDIC AEVGIPFIYK SSYDKANRSS
GKSYRGMGME KGLDILADVK KQLGVPVLTD VHSIEEIPAV AAVVDVLQTP AFLCRQTDFI
HAVASCGRPV NIKKGQFLAP GDMKNVVDKA REANGGADNI MVCERGASFG YNNLVSDMRS
LAIMRETGCP VVFDATHSVQ LPGGQGTASG GQREFVPVLA RAAVAVGVAG LFMETHPNPA
QALSDGPNAW PLPRMKALLS TLKAIDELVK SRGLLETEA