ID   KDSB_CHLT3              Reviewed;         246 AA.
AC   B3QTV9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=Ctha_1850;
OS   Chloroherpeton thalassium (strain ATCC 35110 / GB-78).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chloroherpeton.
OX   NCBI_TaxID=517418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35110 / GB-78;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Chloroherpeton thalassium ATCC 35110.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001100; ACF14307.1; -; Genomic_DNA.
DR   RefSeq; WP_012500391.1; NC_011026.1.
DR   AlphaFoldDB; B3QTV9; -.
DR   SMR; B3QTV9; -.
DR   STRING; 517418.Ctha_1850; -.
DR   EnsemblBacteria; ACF14307; ACF14307; Ctha_1850.
DR   KEGG; cts:Ctha_1850; -.
DR   eggNOG; COG1212; Bacteria.
DR   HOGENOM; CLU_065038_0_1_10; -.
DR   OMA; FMATCAK; -.
DR   OrthoDB; 1345588at2; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00358; UER00476.
DR   Proteomes; UP000001208; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008690; F:3-deoxy-manno-octulosonate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Cytoplasm; Lipopolysaccharide biosynthesis; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..246
FT                   /note="3-deoxy-manno-octulosonate cytidylyltransferase"
FT                   /id="PRO_0000370047"
SQ   SEQUENCE   246 AA;  27172 MW;  0170B54D9E048B94 CRC64;
     MKAVIVIPAR LKSTRLPEKM LVDLDGKPLV VRTYEQAKKS RLASDVLLAV DSKRLLDIAE
     SFGCKAVLTP ENLQSGTDRI AFAAKSIDAD VVINVQGDEP LIPPEMIDSA ILPFIENAAL
     PCATLIQPIV SDVPEILQNP NVVKVVTDKN GYALYFSRSP IPYQRNSDAQ PKIFRHIGLY
     AFRKPALETF TTLPPSMLEE TERLEQLRLL ENGIRIKCVI TNLDSQAVDT ADDLAKVKAI
     LAKKLK