KDSB_PSEAE
ID KDSB_PSEAE Reviewed; 254 AA.
AC Q9HZM5;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, 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=PA2979;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(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; AE004091; AAG06367.1; -; Genomic_DNA.
DR PIR; C83274; C83274.
DR RefSeq; NP_251669.1; NC_002516.2.
DR RefSeq; WP_003106922.1; NZ_QZGE01000009.1.
DR PDB; 4XWI; X-ray; 1.92 A; A/B=1-254.
DR PDBsum; 4XWI; -.
DR AlphaFoldDB; Q9HZM5; -.
DR SMR; Q9HZM5; -.
DR STRING; 287.DR97_4960; -.
DR PaxDb; Q9HZM5; -.
DR PRIDE; Q9HZM5; -.
DR EnsemblBacteria; AAG06367; AAG06367; PA2979.
DR GeneID; 880169; -.
DR KEGG; pae:PA2979; -.
DR PATRIC; fig|208964.12.peg.3126; -.
DR PseudoCAP; PA2979; -.
DR HOGENOM; CLU_065038_1_0_6; -.
DR InParanoid; Q9HZM5; -.
DR OMA; FMATCAK; -.
DR PhylomeDB; Q9HZM5; -.
DR BioCyc; PAER208964:G1FZ6-3031-MON; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00358; UER00476.
DR Proteomes; UP000002438; 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 CHAIN 1..254
FT /note="3-deoxy-manno-octulosonate cytidylyltransferase"
FT /id="PRO_0000188510"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:4XWI"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:4XWI"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:4XWI"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4XWI"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:4XWI"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:4XWI"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:4XWI"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4XWI"
FT HELIX 77..88
FT /evidence="ECO:0007829|PDB:4XWI"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:4XWI"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:4XWI"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:4XWI"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:4XWI"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:4XWI"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:4XWI"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:4XWI"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:4XWI"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:4XWI"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:4XWI"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:4XWI"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:4XWI"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:4XWI"
FT HELIX 242..251
FT /evidence="ECO:0007829|PDB:4XWI"
SQ SEQUENCE 254 AA; 27646 MW; 6E553B70DE2446AE CRC64;
MTQAFTVVIP ARYASTRLPG KPLQDIAGQP MIQRVWNQAR KSAASRVVVA TDDERILAAC
QGFGAEALLT RAEHNSGTDR LEEVASRLGL ASDAIVVNVQ GDEPLIPPAL IDQVAANLAA
HPEAAIATLA EPIHEVSALF NPNVVKVATD IDGLALTFSR APLPWARDAF ARDRDSLPEG
VPYRRHIGIY AYRVGFLADF VAWGPCWLEN AESLEQLRAL WHGVRIHVAD ARENMLPGVD
TPEDLERVRR VLGG
