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Database: UniProt
Entry: R6CWF6_9BACE
LinkDB: R6CWF6_9BACE
Original site: R6CWF6_9BACE 
ID   R6CWF6_9BACE            Unreviewed;       254 AA.
AC   R6CWF6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=3-deoxy-manno-octulosonate cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_00057};
DE            EC=2.7.7.38 {ECO:0000256|HAMAP-Rule:MF_00057};
DE   AltName: Full=CMP-2-keto-3-deoxyoctulosonic acid synthase {ECO:0000256|HAMAP-Rule:MF_00057};
DE            Short=CKS {ECO:0000256|HAMAP-Rule:MF_00057};
DE            Short=CMP-KDO synthase {ECO:0000256|HAMAP-Rule:MF_00057};
GN   Name=kdsB {ECO:0000256|HAMAP-Rule:MF_00057};
GN   ORFNames=BN697_00019 {ECO:0000313|EMBL:CDA77174.1};
OS   Bacteroides sp. CAG:530.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1262741 {ECO:0000313|EMBL:CDA77174.1, ECO:0000313|Proteomes:UP000018392};
RN   [1] {ECO:0000313|EMBL:CDA77174.1, ECO:0000313|Proteomes:UP000018392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:530 {ECO:0000313|Proteomes:UP000018392};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:0000256|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:0000256|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:0000256|HAMAP-
CC       Rule:MF_00057}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00057}.
CC   -!- SIMILARITY: Belongs to the KdsB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00057}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDA77174.1}.
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DR   EMBL; CBCL010000140; CDA77174.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6CWF6; -.
DR   UniPathway; UPA00358; UER00476.
DR   Proteomes; UP000018392; Unassembled WGS sequence.
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   HAMAP; MF_00057; KdsB; 1.
DR   InterPro; IPR003329; Cytidylyl_trans.
DR   InterPro; IPR004528; KdsB.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   NCBIfam; TIGR00466; kdsB; 1.
DR   PANTHER; PTHR42866; 3-DEOXY-MANNO-OCTULOSONATE CYTIDYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR42866:SF2; 3-DEOXY-MANNO-OCTULOSONATE CYTIDYLYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02348; CTP_transf_3; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00057};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985,
KW   ECO:0000256|HAMAP-Rule:MF_00057};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00057}; Reference proteome {ECO:0000313|Proteomes:UP000018392};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00057}.
SQ   SEQUENCE   254 AA;  28342 MW;  0039E48818F2F1FF CRC64;
     MKFIGIIPAR YASTRFPAKP LALLGGKTVI QRVYEQVAGV LDEAYVATDD ERIEQAVKEF
     GGKVVMTSVN HKSGTDRCYE AYTKVGSGYD VVVNIQGDEP FIQPSQLEAI KNCFNDPSTD
     IATLVKPFTP ADGFEALENV NSPKVVVNKN MNALYFSRSI IPYQRNKDKA EWLAGHTYYK
     HIGLYAYRAE VLKQITSLPQ SSLELAESLE QLRWLENGYS IKVGISEVET IGIDTPQDLA
     RAEEFLKEHG DVKL
//
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