KDSB_SHEFN
ID KDSB_SHEFN Reviewed; 245 AA.
AC Q083F6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=Sfri_1759;
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400;
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 Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-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; CP000447; ABI71609.1; -; Genomic_DNA.
DR RefSeq; WP_011637225.1; NC_008345.1.
DR AlphaFoldDB; Q083F6; -.
DR SMR; Q083F6; -.
DR STRING; 318167.Sfri_1759; -.
DR EnsemblBacteria; ABI71609; ABI71609; Sfri_1759.
DR KEGG; sfr:Sfri_1759; -.
DR eggNOG; COG1212; Bacteria.
DR HOGENOM; CLU_065038_0_1_6; -.
DR OMA; MSIKEHE; -.
DR OrthoDB; 1345588at2; -.
DR UniPathway; UPA00030; -.
DR Proteomes; UP000000684; 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 Reference proteome; Transferase.
FT CHAIN 1..245
FT /note="8-amino-3,8-dideoxy-manno-octulosonate
FT cytidylyltransferase"
FT /id="PRO_0000370149"
SQ SEQUENCE 245 AA; 27521 MW; 1834369E04285973 CRC64;
MKVTLLIPAR YGSSRFPGKP LAPINGKPMI QHVYERASLA KGLDSIYVAT DDDRIKDAVE
SFGGKVVMTS PDAASGTDRI NDAIALLGLN DDDLVINLQG DQPLIDPISI EQIISLFERH
PGEFEMATLG FEIVDKRELD DPMHVKMVFD NDHNALYFSR SRIPFGRDTN DYPVYKHLGV
YAYTKRFVNA FAKLPLGRLE DLEKLEQLRA LEYGHKIKIA ISAFDSPEVD TPEDIRKCEL
RLAVD
