KDSB_ECOLI
ID KDSB_ECOLI Reviewed; 248 AA.
AC P04951;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 184.
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};
GN OrderedLocusNames=b0918, JW0901;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=K12;
RX PubMed=3023327; DOI=10.1016/s0021-9258(18)66638-4;
RA Goldman R.C., Bolling T.J., Kohlbrenner W.E., Kim Y., Fox J.L.;
RT "Primary structure of CTP:CMP-3-deoxy-D-manno-octulosonate
RT cytidylyltransferase (CMP-KDO synthetase) from Escherichia coli.";
RL J. Biol. Chem. 261:15831-15835(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
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 -!- INTERACTION:
CC P04951; P67430: nemR; NbExp=3; IntAct=EBI-544810, EBI-544803;
CC P04951; P0ACU2: rutR; NbExp=2; IntAct=EBI-544810, EBI-1121539;
CC P04951; P0CE47: tufA; NbExp=2; IntAct=EBI-544810, EBI-301077;
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; J02614; AAA83877.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74004.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35664.1; -; Genomic_DNA.
DR PIR; A26322; A26322.
DR RefSeq; NP_415438.1; NC_000913.3.
DR RefSeq; WP_000011603.1; NZ_LN832404.1.
DR PDB; 1VH1; X-ray; 2.60 A; A/B/C/D=2-248.
DR PDB; 3K8D; X-ray; 1.90 A; A/B/C/D=1-248.
DR PDB; 3K8E; X-ray; 2.51 A; A/B/C/D=1-248.
DR PDBsum; 1VH1; -.
DR PDBsum; 3K8D; -.
DR PDBsum; 3K8E; -.
DR AlphaFoldDB; P04951; -.
DR SMR; P04951; -.
DR BioGRID; 4260010; 226.
DR BioGRID; 849913; 2.
DR DIP; DIP-10066N; -.
DR IntAct; P04951; 20.
DR STRING; 511145.b0918; -.
DR SWISS-2DPAGE; P04951; -.
DR jPOST; P04951; -.
DR PaxDb; P04951; -.
DR PRIDE; P04951; -.
DR EnsemblBacteria; AAC74004; AAC74004; b0918.
DR EnsemblBacteria; BAA35664; BAA35664; BAA35664.
DR GeneID; 945539; -.
DR KEGG; ecj:JW0901; -.
DR KEGG; eco:b0918; -.
DR PATRIC; fig|1411691.4.peg.1358; -.
DR EchoBASE; EB0514; -.
DR eggNOG; COG1212; Bacteria.
DR HOGENOM; CLU_065038_1_0_6; -.
DR InParanoid; P04951; -.
DR OMA; FMATCAK; -.
DR PhylomeDB; P04951; -.
DR BioCyc; EcoCyc:CPM-KDOSYNTH-MON; -.
DR BioCyc; MetaCyc:CPM-KDOSYNTH-MON; -.
DR BRENDA; 2.7.7.38; 2026.
DR SABIO-RK; P04951; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00358; UER00476.
DR EvolutionaryTrace; P04951; -.
DR PRO; PR:P04951; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008690; F:3-deoxy-manno-octulosonate cytidylyltransferase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0033468; P:CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IDA:EcoCyc.
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; Direct protein sequencing;
KW Lipopolysaccharide biosynthesis; Magnesium; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..248
FT /note="3-deoxy-manno-octulosonate cytidylyltransferase"
FT /id="PRO_0000188501"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:3K8D"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:3K8D"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3K8D"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:3K8E"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:3K8D"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:3K8D"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:3K8D"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:3K8D"
FT HELIX 75..86
FT /evidence="ECO:0007829|PDB:3K8D"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:3K8D"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:3K8D"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:3K8D"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:3K8D"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:3K8D"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:3K8D"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:3K8D"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:3K8D"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:3K8D"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:3K8D"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:3K8D"
FT HELIX 212..216
FT /evidence="ECO:0007829|PDB:3K8D"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:3K8D"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:3K8D"
SQ SEQUENCE 248 AA; 27614 MW; AAB3CFDF4841FE7A CRC64;
MSFVVIIPAR YASTRLPGKP LVDINGKPMI VHVLERARES GAERIIVATD HEDVARAVEA
AGGEVCMTRA DHQSGTERLA EVVEKCAFSD DTVIVNVQGD EPMIPATIIR QVADNLAQRQ
VGMATLAVPI HNAEEAFNPN AVKVVLDAEG YALYFSRATI PWDRDRFAEG LETVGDNFLR
HLGIYGYRAG FIRRYVNWQP SPLEHIEMLE QLRVLWYGEK IHVAVAQEVP GTGVDTPEDL
ERVRAEMR
