ID   KDSB2_BURL3             Reviewed;         265 AA.
AC   Q39M82;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=3-deoxy-manno-octulosonate cytidylyltransferase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00057};
DE            Short=CKS 2 {ECO:0000255|HAMAP-Rule:MF_00057};
DE            Short=CMP-KDO synthase 2 {ECO:0000255|HAMAP-Rule:MF_00057};
GN   Name=kdsB2 {ECO:0000255|HAMAP-Rule:MF_00057};
GN   OrderedLocusNames=Bcep18194_C7390;
OS   Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS   R18194 / 383).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=482957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 3 of Burkholderia sp. 383.";
RL   Submitted (OCT-2005) 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; CP000150; ABB06434.1; -; Genomic_DNA.
DR   RefSeq; WP_011350077.1; NC_007509.1.
DR   AlphaFoldDB; Q39M82; -.
DR   SMR; Q39M82; -.
DR   EnsemblBacteria; ABB06434; ABB06434; Bcep18194_C7390.
DR   GeneID; 45092763; -.
DR   KEGG; bur:Bcep18194_C7390; -.
DR   PATRIC; fig|482957.22.peg.7983; -.
DR   HOGENOM; CLU_065038_1_0_4; -.
DR   OMA; MSIKEHE; -.
DR   OrthoDB; 1345588at2; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00358; UER00476.
DR   Proteomes; UP000002705; Chromosome 3.
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   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   Transferase.
FT   CHAIN           1..265
FT                   /note="3-deoxy-manno-octulosonate cytidylyltransferase 2"
FT                   /id="PRO_0000370040"
SQ   SEQUENCE   265 AA;  28270 MW;  E834EF91930A7646 CRC64;
     MTSFNSGRPV HVVIPARYGS TRLPGKPLVD LAGEPMIARV HARVSRALPG ADIVVAIDDA
     RIAAALDARG IRFAMTGAHH ASGTDRAAEL ARVSGWHDTD VVLNVQGDEP LVPEALLKAF
     ADFCVAAPDL GIATVACPVG DAALLDEPGI VKLVVDRRGR ALYFSRAAIP FCRDGRSAGA
     DLGGHLRHIG LYGYSNAALQ ALAHTAPCEL EQLEQLEQLR ALWLGMPIDV MRWPDAPPAG
     VDTPDDVARV VSLLKRQTQD ETEPY