ID   KDSB_SHESW              Reviewed;         245 AA.
AC   A1RJ74;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=Sputw3181_1884;
OS   Shewanella sp. (strain W3-18-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=351745;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W3-18-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. W3-18-1.";
RL   Submitted (DEC-2006) 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; CP000503; ABM24719.1; -; Genomic_DNA.
DR   RefSeq; WP_011789211.1; NC_008750.1.
DR   AlphaFoldDB; A1RJ74; -.
DR   SMR; A1RJ74; -.
DR   PRIDE; A1RJ74; -.
DR   KEGG; shw:Sputw3181_1884; -.
DR   HOGENOM; CLU_065038_0_1_6; -.
DR   OMA; MSIKEHE; -.
DR   UniPathway; UPA00030; -.
DR   Proteomes; UP000002597; 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_0000370160"
SQ   SEQUENCE   245 AA;  27368 MW;  203DD76DF9714083 CRC64;
     MNVILLIPAR YGSSRFPGKP LAPINGKPMI QHVYERASLA KGLTNIYVAT DDERIKATVE
     GFGGKVVMTS PDAASGTDRI NEAIKLLGLK DDDLVINVQG DQPLIDPTAI EQLINLFERQ
     PGEFEMATLG YEIVNKADID DPMQVKMVFD NNYYALYFSR SRIPFGRDTQ DYPVFKHLGI
     YAYTSKFVQT FAALPLGRLE DLEKLEQLRA LEHGHKIKIA ISASNSLEVD RPEDIHKCEQ
     RLAAG