ID   KDSB_SHEPW              Reviewed;         245 AA.
AC   B8CMP6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=swp_2705;
OS   Shewanella piezotolerans (strain WP3 / JCM 13877).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=225849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP3 / JCM 13877;
RX   PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA   Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA   Bartlett D.H., Yu J., Hu S., Xiao X.;
RT   "Environmental adaptation: genomic analysis of the piezotolerant and
RT   psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT   WP3.";
RL   PLoS ONE 3:E1937-E1937(2008).
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; CP000472; ACJ29436.1; -; Genomic_DNA.
DR   RefSeq; WP_020912792.1; NC_011566.1.
DR   AlphaFoldDB; B8CMP6; -.
DR   SMR; B8CMP6; -.
DR   STRING; 225849.swp_2705; -.
DR   EnsemblBacteria; ACJ29436; ACJ29436; swp_2705.
DR   KEGG; swp:swp_2705; -.
DR   eggNOG; COG1212; Bacteria.
DR   HOGENOM; CLU_065038_0_1_6; -.
DR   OMA; MSIKEHE; -.
DR   OrthoDB; 1345588at2; -.
DR   UniPathway; UPA00030; -.
DR   Proteomes; UP000000753; 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_0000370154"
SQ   SEQUENCE   245 AA;  27347 MW;  018D87A132AEB1F0 CRC64;
     MNVTLLIPAR YGSSRFPGKP LAPINGKPMI QHVYERASLA KGLTDIYVAT DDDRIKDAVE
     GFGGKVVMTS AEAASGTDRI EDAITQLGLA EDDLVVNLQG DQPLIDPISI EQIISLFERH
     PGEFGMATLG FQITEEEELN DPKHVKLVFD NEFNALYFSR ARIPFGRDTD DYPVYKHLGV
     YAYTRKFVQT FAKLPLGRLE DLEKLEQLRA LEHGHKIKVA ISAFDSPEVD TPEDIRICEA
     RLAVD