KDSB_ACIBT
ID KDSB_ACIBT Reviewed; 253 AA.
AC A3M4Z0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 92.
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=A1S_1557;
OS Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS KC755 / 5377).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=400667;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX PubMed=17344419; DOI=10.1101/gad.1510307;
RA Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA Gerstein M., Snyder M.;
RT "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT density pyrosequencing and transposon mutagenesis.";
RL Genes Dev. 21:601-614(2007).
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; CP000521; ABO11984.2; -; Genomic_DNA.
DR RefSeq; WP_000680696.1; NZ_CP053098.1.
DR PDB; 3POL; X-ray; 2.30 A; A=1-253.
DR PDB; 4FCU; X-ray; 1.90 A; A=1-253.
DR PDBsum; 3POL; -.
DR PDBsum; 4FCU; -.
DR AlphaFoldDB; A3M4Z0; -.
DR SMR; A3M4Z0; -.
DR GeneID; 66397363; -.
DR KEGG; acb:A1S_1557; -.
DR HOGENOM; CLU_065038_1_0_6; -.
DR BRENDA; 2.7.7.38; 98.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00358; UER00476.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008690; F:3-deoxy-manno-octulosonate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
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; Transferase.
FT CHAIN 1..253
FT /note="3-deoxy-manno-octulosonate cytidylyltransferase"
FT /id="PRO_0000369985"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:4FCU"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:4FCU"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:4FCU"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:4FCU"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:4FCU"
FT HELIX 52..59
FT /evidence="ECO:0007829|PDB:4FCU"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:4FCU"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:4FCU"
FT HELIX 75..86
FT /evidence="ECO:0007829|PDB:4FCU"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:4FCU"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:4FCU"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:4FCU"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:4FCU"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:4FCU"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:4FCU"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:4FCU"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:4FCU"
FT STRAND 180..189
FT /evidence="ECO:0007829|PDB:4FCU"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:4FCU"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:4FCU"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:4FCU"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:4FCU"
FT HELIX 238..245
FT /evidence="ECO:0007829|PDB:4FCU"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:4FCU"
SQ SEQUENCE 253 AA; 28390 MW; 633E75080505346C CRC64;
MKHIVIPARF SSSRLPGKPL LLIHDRPMIL RVVDQAKKVE GFDDLCVATD DERIAEICRA
EGVDVVLTSA DHPSGTDRLS EVARIKGWDA DDIIVNVQGD EPLLPAQLVQ QVAKLLVDKP
NCSMSTLCEP IHALDEFQRD SIVKVVMSKQ NEALYFSRAT IPYDRDGAKR DEPTLHTQAF
RHLGLYAYRV SLLQEYVTWE MGKLEKLESL EQLRVLENGH RIAIAVAEAN LPPGVDTQAD
LDRLNNMPVE SFE
