KDSB_COXBU
ID KDSB_COXBU Reviewed; 249 AA.
AC Q83E52;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 25-MAY-2022, entry version 111.
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=CBU_0479;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO90028.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE016828; AAO90028.2; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_819514.2; NC_002971.3.
DR PDB; 3TQD; X-ray; 1.80 A; A=1-249.
DR PDBsum; 3TQD; -.
DR AlphaFoldDB; Q83E52; -.
DR SMR; Q83E52; -.
DR STRING; 227377.CBU_0479; -.
DR DNASU; 1208363; -.
DR EnsemblBacteria; AAO90028; AAO90028; CBU_0479.
DR GeneID; 1208363; -.
DR KEGG; cbu:CBU_0479; -.
DR PATRIC; fig|227377.7.peg.470; -.
DR eggNOG; COG1212; Bacteria.
DR HOGENOM; CLU_065038_1_0_6; -.
DR OMA; FMATCAK; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00358; UER00476.
DR EvolutionaryTrace; Q83E52; -.
DR Proteomes; UP000002671; 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..249
FT /note="3-deoxy-manno-octulosonate cytidylyltransferase"
FT /id="PRO_0000370051"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:3TQD"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3TQD"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:3TQD"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:3TQD"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:3TQD"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:3TQD"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:3TQD"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:3TQD"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:3TQD"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:3TQD"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:3TQD"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:3TQD"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:3TQD"
FT TURN 165..169
FT /evidence="ECO:0007829|PDB:3TQD"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3TQD"
FT STRAND 181..190
FT /evidence="ECO:0007829|PDB:3TQD"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:3TQD"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:3TQD"
FT HELIX 214..218
FT /evidence="ECO:0007829|PDB:3TQD"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:3TQD"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:3TQD"
SQ SEQUENCE 249 AA; 28025 MW; 5424D4D3D8722816 CRC64;
MEFRVIIPAR FDSTRLPGKA LVDIAGKPMI QHVYESAIKS GAEEVVIATD DKRIRQVAED
FGAVVCMTSS DHQSGTERIA EAAVALGFED DEIIVCLQGD EPLIPPDAIR KLAEDLDEHD
NVKVASLCTP ITEVDELFNP HSTKVVLNRR NYALYFSHAP IPWGRDTFSD KENLQLNGSH
YRHVGIYAYR VGFLEEYLSW DACPAEKMEA LEQLRILWHG GRIHMVVAKS KCPPGVDTEE
DLERVRAYF
