KDSA_RHILO
ID KDSA_RHILO Reviewed; 277 AA.
AC Q98MZ6;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase;
DE EC=2.5.1.55;
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; OrderedLocusNames=mlr0374;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(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 -!- PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate
CC biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate:
CC step 2/3.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB47967.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000012; BAB47967.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q98MZ6; -.
DR SMR; Q98MZ6; -.
DR STRING; 266835.14021354; -.
DR EnsemblBacteria; BAB47967; BAB47967; BAB47967.
DR KEGG; mlo:mlr0374; -.
DR PATRIC; fig|266835.9.peg.297; -.
DR eggNOG; COG2877; Bacteria.
DR HOGENOM; CLU_036666_0_0_5; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR Proteomes; UP000000552; 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; Transferase.
FT CHAIN 1..277
FT /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT /id="PRO_0000187155"
SQ SEQUENCE 277 AA; 29368 MW; 9E4657D6EBCD7ED2 CRC64;
MAPNSSVTVG NVVFDNNAAL ALIAGPCQFE SRQHAFDMAG ALKELTARLG IGLVYKTSYD
KANRTSLSAT RGAGMDAALP VFDELRKEFS LPVLTDVHTE EQCAIVAPHV DVLQIPAFLS
RQTDMLVAAA KTGKVINVKK GQFLAPWDMK NVVAKITGSG NPNVLTTERG ASFGYNTLVS
DMRALPVMAE IGAPVIFDAT HSVQQPGGQG GSSGGERRFV ETLARAAVAV GVAGVFIETH
QDPDNSTSSD GPNMLPLKDM PALLERLMAF DRIAKGR
