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}.
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; 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