KDSB_SHEWM
ID KDSB_SHEWM Reviewed; 245 AA.
AC B1KDR7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=Swoo_2182;
OS Shewanella woodyi (strain ATCC 51908 / MS32).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=392500;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51908 / MS32;
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 Lykidis A., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella woodyi ATCC 51908.";
RL Submitted (FEB-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; CP000961; ACA86464.1; -; Genomic_DNA.
DR RefSeq; WP_012324808.1; NC_010506.1.
DR AlphaFoldDB; B1KDR7; -.
DR SMR; B1KDR7; -.
DR STRING; 392500.Swoo_2182; -.
DR EnsemblBacteria; ACA86464; ACA86464; Swoo_2182.
DR KEGG; swd:Swoo_2182; -.
DR eggNOG; COG1212; Bacteria.
DR HOGENOM; CLU_065038_0_1_6; -.
DR OMA; MSIKEHE; -.
DR OrthoDB; 1345588at2; -.
DR UniPathway; UPA00030; -.
DR Proteomes; UP000002168; 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_0000370161"
SQ SEQUENCE 245 AA; 27314 MW; 33A4EE4DDE8CA993 CRC64;
MNVTLLIPAR YGSSRFPGKP LAPINGKPMI QHVYERASLA KGLTAIYVAT DDDRIKEAVE
AFGGKVVMTD PQAASGTDRI EDAITQLGLK DDDLIVNLQG DQPLIDPISI EQVITLFERH
PGEFSMATLG VEITEKAELD DPKHVKMVFD NNFNALYFSR ARIPFGRDTN DYPVYKHLGI
YAYTRSFIST FAKLPLGRLE DLEKLEQLRA LEHGHKIKVA ISAFDSPEVD TPEDIRICEA
RLAVD
