ID L2F5S6_9GAMM Unreviewed; 276 AA.
AC L2F5S6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=MOMA_06801 {ECO:0000313|EMBL:ELA08250.1};
OS Moraxella macacae 0408225.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=1230338 {ECO:0000313|EMBL:ELA08250.1, ECO:0000313|Proteomes:UP000023795};
RN [1] {ECO:0000313|EMBL:ELA08250.1, ECO:0000313|Proteomes:UP000023795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0408225 {ECO:0000313|EMBL:ELA08250.1,
RC ECO:0000313|Proteomes:UP000023795};
RX PubMed=23409273;
RA Ladner J.T., Whitehouse C.A., Koroleva G.I., Palacios G.F.;
RT "Genome Sequence of Moraxella macacae 0408225, a Novel Bacterial Species
RT Isolated from a Cynomolgus Macaque with Epistaxis.";
RL Genome Announc. 1:E00188-12(2013).
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:ELA08250.1}.
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DR EMBL; ANIN01000002; ELA08250.1; -; Genomic_DNA.
DR RefSeq; WP_009501800.1; NZ_ANIN01000002.1.
DR AlphaFoldDB; L2F5S6; -.
DR STRING; 1230338.MOMA_06801; -.
DR PATRIC; fig|1230338.3.peg.1452; -.
DR eggNOG; COG1212; Bacteria.
DR OrthoDB; 9815559at2; -.
DR UniPathway; UPA00358; UER00476.
DR Proteomes; UP000023795; 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:UP000023795};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00057}.
SQ SEQUENCE 276 AA; 30710 MW; EA77E7C5BF625EE6 CRC64;
MKKHIVIPAR LKSTRLPNKP LLHIHGKPMI LWVIDRACAV QQAGIADDIF VATDDDSIAK
VCREYCQSHA CDTKTSVNIV MTDPNHASGT DRLAQVALQQ AWADHDIVIN MQGDEPLIPI
KLIAQVTNLL LHKTDCVMAT LAEPIVTFEE FYRSSVVKVV KNQHNEALYF SRSPIPCDRN
ALPTNLPTDT PPNPTDTPIN ALRHLGLYAY KVALLHQFAQ WQQGQLECLE GLEQLRVIEH
GHKIALDIAC AMLPCGVDTQ CDLDRLNAMD LSAFVD
//