ID   KDSB_SHESH              Reviewed;         245 AA.
AC   A8FW10;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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}; OrderedLocusNames=Ssed_2424;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
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., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-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}.
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; CP000821; ABV37033.1; -; Genomic_DNA.
DR   RefSeq; WP_012142768.1; NC_009831.1.
DR   AlphaFoldDB; A8FW10; -.
DR   SMR; A8FW10; -.
DR   STRING; 425104.Ssed_2424; -.
DR   EnsemblBacteria; ABV37033; ABV37033; Ssed_2424.
DR   KEGG; sse:Ssed_2424; -.
DR   eggNOG; COG1212; Bacteria.
DR   HOGENOM; CLU_065038_0_1_6; -.
DR   OMA; MSIKEHE; -.
DR   OrthoDB; 1345588at2; -.
DR   UniPathway; UPA00030; -.
DR   Proteomes; UP000002015; 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_0000370156"
SQ   SEQUENCE   245 AA;  27310 MW;  F8B1F1A9D4571A57 CRC64;
     MNVTLLIPAR YGSSRFPGKP LAPINGKPMI QHVYERASLA KGLTAIYVAT DDDRIKDAVE
     GFGGKVVMTS PDAASGTDRI EDAITQLGLK DDDLVVNLQG DQPLIDPISI EQIISLFERH
     PGEFGMATLG FEITEKCELD DPKHVKMVFD NEFNALYFSR ARIPFGRDTN DYPVYKHLGV
     YAYTRSFIST FAKLPLGRLE DLEKLEQLRA LEHGYKIKVA ISAFDSPEVD TPEDIRVCES
     RLAVD