ID A0A495AI11_9ENTR Unreviewed; 248 AA.
AC A0A495AI11;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=D8M09_10995 {ECO:0000313|EMBL:RKQ39707.1};
OS Enterobacter sp. R1(2018).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=2447891 {ECO:0000313|EMBL:RKQ39707.1, ECO:0000313|Proteomes:UP000271976};
RN [1] {ECO:0000313|EMBL:RKQ39707.1, ECO:0000313|Proteomes:UP000271976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1(2018) {ECO:0000313|Proteomes:UP000271976};
RA Ontanon O.M., Ghio S., Rivarola M., Campos E.;
RT "Enterobacter sp. from a bacterial cellulose degrading consortium draft
RT genome.";
RL Submitted (OCT-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:RKQ39707.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RCAA01000035; RKQ39707.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495AI11; -.
DR OrthoDB; 9815559at2; -.
DR UniPathway; UPA00358; UER00476.
DR Proteomes; UP000271976; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00057}.
SQ SEQUENCE 248 AA; 27642 MW; DA05845E35FB187A CRC64;
MSFVAIIPAR YSSTRLPGKP LKDINGKPMV VHVLERARES GAERIIVATD HEEVARAVEA
AGGEVCMTRA DHQSGTERLA EVIEKCGFSD DTIIVNVQGD EPMIPPVIIR QVAENLANCQ
AGMATLAVPI DSAEEAFNPN AVKVVMDAQG YALYFSRATI PWDRDRFARS REKIGDTFLR
HIGIYGYRAG FIRRYVSWEP SQLEQIEMLE QLRVLWNGEK IHVAVAKEIP GIGVDTPEDL
ERIRVAMR
//
