KDSA_HELPY
ID KDSA_HELPY Reviewed; 276 AA.
AC P56060;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 116.
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=HP_0003;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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}.
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DR EMBL; AE000511; AAD07076.1; -; Genomic_DNA.
DR PIR; C64520; C64520.
DR RefSeq; NP_206805.1; NC_000915.1.
DR RefSeq; WP_000858181.1; NC_018939.1.
DR PDB; 4Z1A; X-ray; 2.00 A; A/B=1-276.
DR PDB; 4Z1B; X-ray; 2.40 A; A/B=1-276.
DR PDB; 4Z1C; X-ray; 1.93 A; A/B=1-276.
DR PDB; 4Z1D; X-ray; 1.65 A; A/B=1-276.
DR PDBsum; 4Z1A; -.
DR PDBsum; 4Z1B; -.
DR PDBsum; 4Z1C; -.
DR PDBsum; 4Z1D; -.
DR AlphaFoldDB; P56060; -.
DR SMR; P56060; -.
DR STRING; 85962.C694_00015; -.
DR PaxDb; P56060; -.
DR EnsemblBacteria; AAD07076; AAD07076; HP_0003.
DR KEGG; hpy:HP_0003; -.
DR PATRIC; fig|85962.47.peg.3; -.
DR eggNOG; COG2877; Bacteria.
DR OMA; FRGIPTM; -.
DR PhylomeDB; P56060; -.
DR BRENDA; 2.5.1.55; 2604.
DR SABIO-RK; P56060; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR Proteomes; UP000000429; Chromosome.
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:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0046364; P:monosaccharide biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipopolysaccharide biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..276
FT /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT /id="PRO_0000187133"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:4Z1D"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:4Z1D"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:4Z1D"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:4Z1D"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:4Z1A"
FT HELIX 66..80
FT /evidence="ECO:0007829|PDB:4Z1D"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:4Z1D"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4Z1A"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:4Z1D"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:4Z1D"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:4Z1D"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:4Z1D"
FT HELIX 114..122
FT /evidence="ECO:0007829|PDB:4Z1D"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:4Z1D"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:4Z1D"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:4Z1D"
FT HELIX 160..166
FT /evidence="ECO:0007829|PDB:4Z1D"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:4Z1D"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4Z1D"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:4Z1D"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:4Z1D"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:4Z1D"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:4Z1D"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:4Z1D"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:4Z1D"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:4Z1D"
FT HELIX 259..275
FT /evidence="ECO:0007829|PDB:4Z1D"
SQ SEQUENCE 276 AA; 30346 MW; D9161C551AE0FDF9 CRC64;
MKTSKTKTPK SVLIAGPCVI ESLENLRSIA TKLQPLANNE RLDFYFKASF DKANRTSLES
YRGPGLEKGL EMLQTIKEEF GYKILTDVHE SYQASVAAKV ADILQIPAFL CRQTDLIVEV
SQTNAIVNIK KGQFMNPKDM QYSVLKALKT RDKSIQSPTY ETALKNGVWL CERGSSFGYG
NLVVDMRSLK IMREFAPVIF DATHSVQMPG GANGKSSGDS SFAPILARAA AAVGIDGLFA
ETHVDPKNAL SDGANMLKPD ELEQLVTDML KIQNLF
