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Database: UniProt
Entry: A0A1G5R378_9GAMM
LinkDB: A0A1G5R378_9GAMM
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ID   A0A1G5R378_9GAMM        Unreviewed;       251 AA.
AC   A0A1G5R378;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=3-deoxy-manno-octulosonate cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_00057};
DE            EC=2.7.7.38 {ECO:0000256|HAMAP-Rule:MF_00057};
DE   AltName: Full=CMP-2-keto-3-deoxyoctulosonic acid synthase {ECO:0000256|HAMAP-Rule:MF_00057};
DE            Short=CKS {ECO:0000256|HAMAP-Rule:MF_00057};
DE            Short=CMP-KDO synthase {ECO:0000256|HAMAP-Rule:MF_00057};
GN   Name=kdsB {ECO:0000256|HAMAP-Rule:MF_00057};
GN   ORFNames=SAMN03097708_03202 {ECO:0000313|EMBL:SCZ67779.1};
OS   Thiohalomonas denitrificans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalomonadales;
OC   Thiohalomonadaceae; Thiohalomonas.
OX   NCBI_TaxID=415747 {ECO:0000313|EMBL:SCZ67779.1, ECO:0000313|Proteomes:UP000199648};
RN   [1] {ECO:0000313|EMBL:SCZ67779.1, ECO:0000313|Proteomes:UP000199648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLD2 {ECO:0000313|EMBL:SCZ67779.1,
RC   ECO:0000313|Proteomes:UP000199648};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation
CC       into bacterial lipopolysaccharide in Gram-negative bacteria.
CC       {ECO:0000256|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:0000256|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:0000256|HAMAP-
CC       Rule:MF_00057}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00057}.
CC   -!- SIMILARITY: Belongs to the KdsB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00057}.
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DR   EMBL; FMWD01000016; SCZ67779.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5R378; -.
DR   STRING; 415747.SAMN03097708_03202; -.
DR   OrthoDB; 9815559at2; -.
DR   UniPathway; UPA00358; UER00476.
DR   Proteomes; UP000199648; Unassembled WGS sequence.
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   HAMAP; MF_00057; KdsB; 1.
DR   InterPro; IPR003329; Cytidylyl_trans.
DR   InterPro; IPR004528; KdsB.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   NCBIfam; TIGR00466; kdsB; 1.
DR   PANTHER; PTHR42866; 3-DEOXY-MANNO-OCTULOSONATE CYTIDYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR42866:SF2; 3-DEOXY-MANNO-OCTULOSONATE CYTIDYLYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02348; CTP_transf_3; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00057};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985,
KW   ECO:0000256|HAMAP-Rule:MF_00057};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00057}; Reference proteome {ECO:0000313|Proteomes:UP000199648};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00057}.
SQ   SEQUENCE   251 AA;  27517 MW;  29B6A997BA4CED77 CRC64;
     MFRVFIPARY ASQRLPGKPL LPIAGRPMLQ HVYERAVASG AAQVIVVTDD ERIADAVMGF
     GGEVLMTGAH HRSGTERIAE AVSALGLDSS EVVVNLQGDE PLMPADLIRQ VAEDLECLPT
     ADIATLATRI HTAGELFDPH AVKVVMDKDG FALYFSRAVI PWDREAFAVT TEELPPAAEH
     YRHLGLYAYR AGFLSRYVDL PPCSIESMES LEQLRVLWHG GRIHVAEAIT QPGPGVDTEA
     DLNRVRKLLE V
//
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