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KDSB_SHEHH
ID   KDSB_SHEHH              Reviewed;         245 AA.
AC   B0TVJ0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=Shal_2316;
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) 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; CP000931; ABZ76875.1; -; Genomic_DNA.
DR   RefSeq; WP_012277404.1; NC_010334.1.
DR   AlphaFoldDB; B0TVJ0; -.
DR   SMR; B0TVJ0; -.
DR   STRING; 458817.Shal_2316; -.
DR   EnsemblBacteria; ABZ76875; ABZ76875; Shal_2316.
DR   KEGG; shl:Shal_2316; -.
DR   eggNOG; COG1212; Bacteria.
DR   HOGENOM; CLU_065038_0_1_6; -.
DR   OMA; MSIKEHE; -.
DR   OrthoDB; 1345588at2; -.
DR   UniPathway; UPA00030; -.
DR   Proteomes; UP000001317; 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_0000370150"
SQ   SEQUENCE   245 AA;  27234 MW;  CB2DC911B2C20D97 CRC64;
     MNVTLLIPAR YGSSRFPGKP LAPINGKPMI QHVYERAALA KGLKDIYVAT DDERIKNAVE
     GFGGKVVMTG ADAASGTDRI DDAITQLGLA DDDLVINLQG DQPLIDPISI EQLVSLCERH
     PGEFDMATLG VEIRDEAQIN DPNHVKMVFD NNFNALYFSR ATIPFGRESS DYPVYKHLGI
     YAYTRKFIQT FAKLPLGRLE DLEKLEQLRA LEYGYKIKVA ISAFDSPEVD TPEDIRICEA
     RLAVD
 
 
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