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Database: UniProt
Entry: A0A3N1X416_9BURK
LinkDB: A0A3N1X416_9BURK
Original site: A0A3N1X416_9BURK 
ID   A0A3N1X416_9BURK        Unreviewed;       256 AA.
AC   A0A3N1X416;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
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=EC845_2332 {ECO:0000313|EMBL:ROR21510.1};
OS   Comamonas sp. BIGb0124.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=2485130 {ECO:0000313|EMBL:ROR21510.1, ECO:0000313|Proteomes:UP000267274};
RN   [1] {ECO:0000313|EMBL:ROR21510.1, ECO:0000313|Proteomes:UP000267274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BIGb0124 {ECO:0000313|EMBL:ROR21510.1,
RC   ECO:0000313|Proteomes:UP000267274};
RA   Samuel B.;
RT   "Genomic analyses of the natural microbiome of Caenorhabditis elegans.";
RL   Submitted (NOV-2018) 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:ROR21510.1}.
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DR   EMBL; RJVF01000010; ROR21510.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N1X416; -.
DR   OrthoDB; 9815559at2; -.
DR   UniPathway; UPA00358; UER00476.
DR   Proteomes; UP000267274; 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:UP000267274};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00057}.
SQ   SEQUENCE   256 AA;  27188 MW;  7645DC58D2365C32 CRC64;
     MSYTVIIPAR LSSTRLPDKP LALLGGIPMV VRVAERAAQS GASRIVVATD SEAVLAACAA
     HGVEAVATRA DHPSGTDRLA EASVALGLGA DDIVVNVQGD EPLIAPSLID AVAQALAGSP
     APMSTAAHPL ASVEEFGNPN VVKVVLDAGS HALYFSRAGI PFARDFPIET WFEGNGPRRP
     DHPLRHIGIY GYRTRFLQQF PLLARSPLEV TESLEQLRVL WHGHRIAVHV TQDAPGTGVD
     TPQDLARVRA IFDNRG
//
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