KDSB_PELPB
ID KDSB_PELPB Reviewed; 247 AA.
AC B4SES6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=Ppha_2414;
OS Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=324925;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5477 / BU-1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Pelodictyon phaeoclathratiforme BU-1.";
RL Submitted (JUN-2008) 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; CP001110; ACF44602.1; -; Genomic_DNA.
DR RefSeq; WP_012509076.1; NC_011060.1.
DR AlphaFoldDB; B4SES6; -.
DR SMR; B4SES6; -.
DR STRING; 324925.Ppha_2414; -.
DR EnsemblBacteria; ACF44602; ACF44602; Ppha_2414.
DR KEGG; pph:Ppha_2414; -.
DR eggNOG; COG1212; Bacteria.
DR HOGENOM; CLU_065038_0_1_10; -.
DR OMA; FMATCAK; -.
DR OrthoDB; 1345588at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00358; UER00476.
DR Proteomes; UP000002724; 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..247
FT /note="3-deoxy-manno-octulosonate cytidylyltransferase"
FT /id="PRO_1000116892"
SQ SEQUENCE 247 AA; 27432 MW; 9C440ECACA752CF9 CRC64;
MKAVILIPAR LDSSRLDRKM LADLEGEPLI VRTWRQALKS RLAEKVVVAT DSREIAAVLD
ACGAEVVMTS PTASCGTERI AEAARHIEGD VFVNLQGDEP LISPENIDLA LEPFFSENPP
DCSTLVLPLR PDDHVQIEDP HQVKVVMDAK GFALYFSRSA IPFQRNMRPT TIVYRHIGLY
AFSADVLQKF ASLPPSMLEE AESLEQLRLL ENGFRIQCVT TLVDNPGVNT VEDLEQVRRI
IRSSLPG