KDSB_BURMA
ID KDSB_BURMA Reviewed; 263 AA.
AC Q62HI2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=BMA2275;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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; CP000010; AAU49875.1; -; Genomic_DNA.
DR RefSeq; WP_004185994.1; NC_006348.1.
DR RefSeq; YP_103838.1; NC_006348.1.
DR AlphaFoldDB; Q62HI2; -.
DR SMR; Q62HI2; -.
DR STRING; 243160.BMA2275; -.
DR EnsemblBacteria; AAU49875; AAU49875; BMA2275.
DR GeneID; 56594749; -.
DR KEGG; bma:BMA2275; -.
DR PATRIC; fig|243160.12.peg.2343; -.
DR eggNOG; COG1212; Bacteria.
DR HOGENOM; CLU_065038_1_0_4; -.
DR OMA; FMATCAK; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00358; UER00476.
DR Proteomes; UP000006693; Chromosome 1.
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 Transferase.
FT CHAIN 1..263
FT /note="3-deoxy-manno-octulosonate cytidylyltransferase"
FT /id="PRO_0000370027"
SQ SEQUENCE 263 AA; 28758 MW; 5A4CC93F0C4E2AEA CRC64;
MTSPLPFVAV VPARLASTRL PNKPLADLGG KPMVVRVAER AREAGAQQVL VASDAQRVLD
AVREHGFDAV LTRADHPSGT DRLAEVAAKL GFDDDTIVVN VQGDEPLIDP QLVRDVASHL
AAHPSCAIAT AAHPIHEAHE VFNPNYVKVV LDAHGVALYF SRAPIPWSRD AYLPHWPNVA
AMPAPTCPVY RHIGLYAYRA RFLRTYPTLA QAPIEAAEQL EQLRAMWHGE RIAVRVTEHA
PEAGIDTPAD LERVQALFRS RAK