KDSB_THIDA
ID KDSB_THIDA Reviewed; 252 AA.
AC Q3SIR7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=Tbd_1505;
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259;
RX PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ97458.1; -; Genomic_DNA.
DR RefSeq; WP_011312017.1; NC_007404.1.
DR AlphaFoldDB; Q3SIR7; -.
DR SMR; Q3SIR7; -.
DR STRING; 292415.Tbd_1505; -.
DR EnsemblBacteria; AAZ97458; AAZ97458; Tbd_1505.
DR KEGG; tbd:Tbd_1505; -.
DR eggNOG; COG1212; Bacteria.
DR HOGENOM; CLU_065038_1_0_4; -.
DR OMA; FMATCAK; -.
DR OrthoDB; 1345588at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00358; UER00476.
DR Proteomes; UP000008291; 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..252
FT /note="3-deoxy-manno-octulosonate cytidylyltransferase"
FT /id="PRO_1000190750"
SQ SEQUENCE 252 AA; 27232 MW; 2CEA8AB3865A0692 CRC64;
MHFRVVIPAR YGSSRLPGKP LADIGGRPMV LHVLDRALQA GAESVVVATD DARVQAAVEA
AGHQALLTSP DHQSGTERLV EVAETLGWPD DTLVVNVQGD EPLIDPALIR EAARQLVVHT
DAVMATLAHP IHDHADFVNP NVVKVVADEA GYAVYFSRAP IPWPRDAFAA EQPMPHEIGA
LRHIGLYAYR AGFLRTYASL ASSPLERCEM LEQLRVLWHG YRISLGVTPT APAPGVDTAD
DLARVRALFA AV