KDSA_BRUME
ID KDSA_BRUME Reviewed; 277 AA.
AC Q8YHF1;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=BMEI0850;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE008917; AAL52031.1; -; Genomic_DNA.
DR PIR; AD3358; AD3358.
DR RefSeq; WP_002964262.1; NZ_GG703780.1.
DR PDB; 3FS2; X-ray; 1.85 A; A/B=1-277.
DR PDBsum; 3FS2; -.
DR AlphaFoldDB; Q8YHF1; -.
DR SMR; Q8YHF1; -.
DR STRING; 224914.BMEI0850; -.
DR EnsemblBacteria; AAL52031; AAL52031; BMEI0850.
DR GeneID; 45124510; -.
DR KEGG; bme:BMEI0850; -.
DR PATRIC; fig|224914.52.peg.593; -.
DR eggNOG; COG2877; Bacteria.
DR OMA; FRGIPTM; -.
DR PhylomeDB; Q8YHF1; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR EvolutionaryTrace; Q8YHF1; -.
DR Proteomes; UP000000419; Chromosome I.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipopolysaccharide biosynthesis; Transferase.
FT CHAIN 1..277
FT /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT /id="PRO_0000187107"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:3FS2"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:3FS2"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:3FS2"
FT HELIX 33..50
FT /evidence="ECO:0007829|PDB:3FS2"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:3FS2"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:3FS2"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:3FS2"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:3FS2"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:3FS2"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:3FS2"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3FS2"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:3FS2"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:3FS2"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:3FS2"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:3FS2"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:3FS2"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:3FS2"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:3FS2"
FT HELIX 185..190
FT /evidence="ECO:0007829|PDB:3FS2"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:3FS2"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:3FS2"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:3FS2"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:3FS2"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:3FS2"
FT STRAND 234..243
FT /evidence="ECO:0007829|PDB:3FS2"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:3FS2"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:3FS2"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:3FS2"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3FS2"
FT HELIX 260..274
FT /evidence="ECO:0007829|PDB:3FS2"
SQ SEQUENCE 277 AA; 29498 MW; 1C7D6532BA2F0DD8 CRC64;
MVTANSTVKV GNVTFSNSAP LALIAGPCQM ETRDHAFEMA GRLKEMTDKL GIGLVYKSSF
DKANRTSLKA ARGIGLEKAL EVFSDLKKEY GFPVLTDIHT EEQCAAVAPV VDVLQIPAFL
CRQTDLLIAA ARTGRVVNVK KGQFLAPWDM KNVLAKITES GNPNVLATER GVSFGYNTLV
SDMRALPIMA GLGAPVIFDA THSVQQPGGQ GGSTGGQREF VETLARAAVA VGVAGLFIET
HEDPDNAPSD GPNMVPIDKM PALLEKLMAF DRIAKAL
