ID   KDSB_SHEB9              Reviewed;         245 AA.
AC   A9L3N6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=8-amino-3,8-dideoxy-manno-octulosonate cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00057};
DE            EC=2.7.7.90 {ECO:0000255|HAMAP-Rule:MF_00057};
DE   AltName: Full=CMP-8-amino-3,8-dideoxy-manno-octulosonate synthase {ECO:0000255|HAMAP-Rule:MF_00057};
GN   Name=kdsB {ECO:0000255|HAMAP-Rule:MF_00057};
GN   OrderedLocusNames=Sbal195_2478;
OS   Shewanella baltica (strain OS195).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS195;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA   Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS195.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Activates KDO8N (a required 8-carbon sugar) for incorporation
CC       into bacterial lipopolysaccharide in the Shewanella genus.
CC       {ECO:0000255|HAMAP-Rule:MF_00057}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8-amino-3,8-dideoxy-alpha-D-manno-octulosonate + CTP = CMP-8-
CC         amino-3,8-dideoxy-alpha-D-manno-oct-2-ulosonate + diphosphate;
CC         Xref=Rhea:RHEA:49284, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:87091, ChEBI:CHEBI:91089; EC=2.7.7.90;
CC         Evidence={ECO:0000255|HAMAP-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; CP000891; ABX49646.1; -; Genomic_DNA.
DR   RefSeq; WP_012197229.1; NC_009997.1.
DR   AlphaFoldDB; A9L3N6; -.
DR   SMR; A9L3N6; -.
DR   EnsemblBacteria; ABX49646; ABX49646; Sbal195_2478.
DR   GeneID; 11772588; -.
DR   KEGG; sbn:Sbal195_2478; -.
DR   HOGENOM; CLU_065038_0_1_6; -.
DR   OMA; MSIKEHE; -.
DR   UniPathway; UPA00030; -.
DR   Proteomes; UP000000770; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008690; F:3-deoxy-manno-octulosonate cytidylyltransferase activity; IEA:InterPro.
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..245
FT                   /note="8-amino-3,8-dideoxy-manno-octulosonate
FT                   cytidylyltransferase"
FT                   /id="PRO_0000370147"
SQ   SEQUENCE   245 AA;  27433 MW;  C6AB5D1FE750829C CRC64;
     MNVTLLIPAR YGSSRFPGKP LAPINGKPMI QHVYERASLA KGLTNIYVAT DDDRIKAAVE
     GFGGKVVMTS PDAASGTDRI NDAINQLGLK DDDLVINLQG DQPLIDPTSI EQVISLFERH
     PGEFEMATLG FEIVNKAELD DPMHVKMVFD NNNYALYFSR SRIPFGRDTQ DYPVYKHLGV
     YAYTRKFVQA FAALPLGRLE DLEKLEQLRA LEYGHKIKIA ISAFDSIEVD TPEDIRKCEQ
     RLAVD