KDSB_AQUAE
ID KDSB_AQUAE Reviewed; 234 AA.
AC O66914;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=3-deoxy-manno-octulosonate cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00057};
DE EC=2.7.7.38 {ECO:0000255|HAMAP-Rule:MF_00057};
DE AltName: Full=CMP-2-keto-3-deoxyoctulosonic acid synthase {ECO:0000255|HAMAP-Rule:MF_00057};
DE Short=CKS {ECO:0000255|HAMAP-Rule:MF_00057};
DE Short=CMP-KDO synthase {ECO:0000255|HAMAP-Rule:MF_00057};
GN Name=kdsB {ECO:0000255|HAMAP-Rule:MF_00057}; OrderedLocusNames=aq_692;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation
CC into bacterial lipopolysaccharide in Gram-negative bacteria.
CC {ECO:0000255|HAMAP-Rule:MF_00057}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-
CC beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986,
CC ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00057};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-
CC octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-
CC deoxy-D-manno-octulosonate and CTP: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00057}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00057}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00057}.
CC -!- SIMILARITY: Belongs to the KdsB family. {ECO:0000255|HAMAP-
CC Rule:MF_00057}.
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DR EMBL; AE000657; AAC06870.1; -; Genomic_DNA.
DR PIR; F70360; F70360.
DR RefSeq; NP_213474.1; NC_000918.1.
DR RefSeq; WP_010880412.1; NC_000918.1.
DR PDB; 2Y6P; X-ray; 2.10 A; A/B/C=1-234.
DR PDBsum; 2Y6P; -.
DR AlphaFoldDB; O66914; -.
DR SMR; O66914; -.
DR STRING; 224324.aq_692; -.
DR EnsemblBacteria; AAC06870; AAC06870; aq_692.
DR KEGG; aae:aq_692; -.
DR PATRIC; fig|224324.8.peg.556; -.
DR eggNOG; COG1212; Bacteria.
DR HOGENOM; CLU_065038_0_1_0; -.
DR InParanoid; O66914; -.
DR OMA; FMATCAK; -.
DR OrthoDB; 1345588at2; -.
DR BRENDA; 2.7.7.38; 396.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00358; UER00476.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008690; F:3-deoxy-manno-octulosonate cytidylyltransferase activity; IBA:GO_Central.
DR GO; GO:0033468; P:CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02517; CMP-KDO-Synthetase; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR HAMAP; MF_00057; KdsB; 1.
DR InterPro; IPR003329; Cytidylyl_trans.
DR InterPro; IPR004528; KdsB.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF02348; CTP_transf_3; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR00466; kdsB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipopolysaccharide biosynthesis;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..234
FT /note="3-deoxy-manno-octulosonate cytidylyltransferase"
FT /id="PRO_0000188496"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2Y6P"
FT TURN 14..18
FT /evidence="ECO:0007829|PDB:2Y6P"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:2Y6P"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:2Y6P"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:2Y6P"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:2Y6P"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:2Y6P"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:2Y6P"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:2Y6P"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:2Y6P"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:2Y6P"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:2Y6P"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:2Y6P"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:2Y6P"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:2Y6P"
FT STRAND 142..150
FT /evidence="ECO:0007829|PDB:2Y6P"
FT STRAND 164..173
FT /evidence="ECO:0007829|PDB:2Y6P"
FT HELIX 174..182
FT /evidence="ECO:0007829|PDB:2Y6P"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:2Y6P"
FT HELIX 196..201
FT /evidence="ECO:0007829|PDB:2Y6P"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:2Y6P"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:2Y6P"
SQ SEQUENCE 234 AA; 27173 MW; C838A2B7B84437C1 CRC64;
MRRAVIIPAR LGSTRLKEKP LKNLLGKPLI RWVVEGLVKT GERVILATDS ERVKEVVEDL
CEVFLTPSDL PSGSDRVLYV VRDLDVDLII NYQGDEPFVY EEDIKLIFRE LEKGERVVTL
ARKDKEAYER PEDVKVVLDR EGYALYFSRS PIPYFRKNDT FYPLKHVGIY GFRKETLMEF
GAMPPSKLEQ IEGLEQLRLL ENGIKIKVLI TENYYHGVDT EEDLKIVEEK LKNL
