KDSB_VIBCH
ID KDSB_VIBCH Reviewed; 252 AA.
AC Q9KQX2;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=3-deoxy-manno-octulosonate cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00057};
DE EC=2.7.7.38 {ECO:0000255|HAMAP-Rule:MF_00057};
DE AltName: Full=CMP-2-keto-3-deoxyoctulosonic acid synthase {ECO:0000255|HAMAP-Rule:MF_00057};
DE Short=CKS {ECO:0000255|HAMAP-Rule:MF_00057};
DE Short=CMP-KDO synthase {ECO:0000255|HAMAP-Rule:MF_00057};
GN Name=kdsB {ECO:0000255|HAMAP-Rule:MF_00057}; OrderedLocusNames=VC_1875;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation
CC into bacterial lipopolysaccharide in Gram-negative bacteria.
CC {ECO:0000255|HAMAP-Rule:MF_00057}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-
CC beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986,
CC ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00057};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-
CC octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-
CC deoxy-D-manno-octulosonate and CTP: step 1/1. {ECO:0000255|HAMAP-
CC 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; AE003852; AAF95023.1; -; Genomic_DNA.
DR PIR; A82146; A82146.
DR RefSeq; NP_231509.1; NC_002505.1.
DR RefSeq; WP_000011329.1; NZ_LT906614.1.
DR PDB; 3OAM; X-ray; 1.75 A; A/B/C/D=1-252.
DR PDBsum; 3OAM; -.
DR AlphaFoldDB; Q9KQX2; -.
DR SMR; Q9KQX2; -.
DR STRING; 243277.VC_1875; -.
DR DNASU; 2613629; -.
DR EnsemblBacteria; AAF95023; AAF95023; VC_1875.
DR GeneID; 57740510; -.
DR KEGG; vch:VC_1875; -.
DR PATRIC; fig|243277.26.peg.1791; -.
DR eggNOG; COG1212; Bacteria.
DR HOGENOM; CLU_065038_1_0_6; -.
DR OMA; FMATCAK; -.
DR BioCyc; VCHO:VC1875-MON; -.
DR BRENDA; 2.7.7.38; 6626.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00358; UER00476.
DR EvolutionaryTrace; Q9KQX2; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008690; F:3-deoxy-manno-octulosonate cytidylyltransferase activity; IBA:GO_Central.
DR GO; GO:0033468; P:CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IEA:UniProtKB-UniRule.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipopolysaccharide biosynthesis;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..252
FT /note="3-deoxy-manno-octulosonate cytidylyltransferase"
FT /id="PRO_0000188517"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3OAM"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:3OAM"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3OAM"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:3OAM"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:3OAM"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:3OAM"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:3OAM"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:3OAM"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:3OAM"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:3OAM"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:3OAM"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:3OAM"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:3OAM"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:3OAM"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:3OAM"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:3OAM"
FT STRAND 178..188
FT /evidence="ECO:0007829|PDB:3OAM"
FT HELIX 191..197
FT /evidence="ECO:0007829|PDB:3OAM"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:3OAM"
FT HELIX 212..216
FT /evidence="ECO:0007829|PDB:3OAM"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:3OAM"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:3OAM"
SQ SEQUENCE 252 AA; 27722 MW; 10C7A093209CF212 CRC64;
MSFTVVIPAR YQSTRLPGKP LADIGGKPMI QWVYEQAMQA GADRVIIATD DERVEQAVQA
FGGVVCMTSP NHQSGTERLA EVVAKMAIPA DHIVVNVQGD EPLIPPAIIR QVADNLAACS
APMATLAVEI EDEAEVFNPN AVKVITDKSG YALYFSRATI PWDRDNFAKA DKAIVQPLLR
HIGIYAYRAG FINTYLDWQP SQLEKIECLE QLRVLWHGEK IHVAVALEAP PAGVDTPEDL
EVVRRIVAER AQ
