KDSB_HAEIN
ID KDSB_HAEIN Reviewed; 254 AA.
AC P44490;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
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=HI_0058;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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}.
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; L42023; AAC21736.1; -; Genomic_DNA.
DR PIR; G64045; G64045.
DR RefSeq; NP_438231.1; NC_000907.1.
DR RefSeq; WP_005693864.1; NC_000907.1.
DR PDB; 1VH3; X-ray; 2.70 A; A/B/C=2-254.
DR PDB; 1VIC; X-ray; 1.80 A; A/B=2-254.
DR PDB; 3DUV; X-ray; 2.30 A; A/B=1-254.
DR PDBsum; 1VH3; -.
DR PDBsum; 1VIC; -.
DR PDBsum; 3DUV; -.
DR AlphaFoldDB; P44490; -.
DR SMR; P44490; -.
DR STRING; 71421.HI_0058; -.
DR DrugBank; DB04482; Cmp-2-Keto-3-Deoxy-Octulosonic Acid.
DR EnsemblBacteria; AAC21736; AAC21736; HI_0058.
DR KEGG; hin:HI_0058; -.
DR PATRIC; fig|71421.8.peg.58; -.
DR eggNOG; COG1212; Bacteria.
DR HOGENOM; CLU_065038_1_0_6; -.
DR OMA; FMATCAK; -.
DR PhylomeDB; P44490; -.
DR BioCyc; HINF71421:G1GJ1-59-MON; -.
DR BRENDA; 2.7.7.38; 2529.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00358; UER00476.
DR EvolutionaryTrace; P44490; -.
DR Proteomes; UP000000579; Chromosome.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..254
FT /note="3-deoxy-manno-octulosonate cytidylyltransferase"
FT /id="PRO_0000188506"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1VIC"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1VIC"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:1VIC"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1VH3"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:1VIC"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:1VIC"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:1VIC"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1VIC"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:1VIC"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:1VIC"
FT HELIX 106..119
FT /evidence="ECO:0007829|PDB:1VIC"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:1VIC"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:1VIC"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:1VIC"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:1VIC"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:1VIC"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1VIC"
FT STRAND 183..192
FT /evidence="ECO:0007829|PDB:1VIC"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:1VIC"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:1VIC"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:1VIC"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:1VIC"
FT HELIX 241..253
FT /evidence="ECO:0007829|PDB:1VIC"
SQ SEQUENCE 254 AA; 28255 MW; 2FAC2BB15BD961A2 CRC64;
MSFTVIIPAR FASSRLPGKP LADIKGKPMI QHVFEKALQS GASRVIIATD NENVADVAKS
FGAEVCMTSV NHNSGTERLA EVVEKLAIPD NEIIVNIQGD EPLIPPVIVR QVADNLAKFN
VNMASLAVKI HDAEELFNPN AVKVLTDKDG YVLYFSRSVI PYDRDQFMNL QDVQKVQLSD
AYLRHIGIYA YRAGFIKQYV QWAPTQLENL EKLEQLRVLY NGERIHVELA KEVPAVGVDT
AEDLEKVRAI LAAN
