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Database: UniProt
Entry: A0A076HUU1_9BACT
LinkDB: A0A076HUU1_9BACT
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ID   A0A076HUU1_9BACT        Unreviewed;       250 AA.
AC   A0A076HUU1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=N008_16145 {ECO:0000313|EMBL:AII53500.1};
OS   Hymenobacter sp. APR13.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1356852 {ECO:0000313|EMBL:AII53500.1, ECO:0000313|Proteomes:UP000028590};
RN   [1] {ECO:0000313|EMBL:AII53500.1, ECO:0000313|Proteomes:UP000028590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APR13 {ECO:0000313|EMBL:AII53500.1,
RC   ECO:0000313|Proteomes:UP000028590};
RA   Li P., Jiang J., Kwok A.H.Y., Lou X., Xu D., Leung F.C.C.;
RT   "Complete genome sequence assembly of Hymenobacter sp. APR13.";
RL   Submitted (JUL-2013) 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; CP006587; AII53500.1; -; Genomic_DNA.
DR   RefSeq; WP_044017399.1; NZ_CP006587.1.
DR   AlphaFoldDB; A0A076HUU1; -.
DR   STRING; 1356852.N008_16145; -.
DR   KEGG; hym:N008_16145; -.
DR   eggNOG; COG1212; Bacteria.
DR   HOGENOM; CLU_065038_0_1_10; -.
DR   OrthoDB; 9815559at2; -.
DR   UniPathway; UPA00358; UER00476.
DR   Proteomes; UP000028590; Chromosome.
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:UP000028590};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00057}.
SQ   SEQUENCE   250 AA;  27987 MW;  1A7D06B2409F8712 CRC64;
     MLAIGIIPAR FASTRLPGKP LVDLGGQTMI ERVVRRAQQS SLSRVVVATD DQRILEHVRG
     FGGEAVLTHP DHPSGTDRVR DAYEQLGVQA DCIVNIQGDE PFIHPSQIDA LVQLFAAPAP
     PQLATLVKPV ISEEELFSPH LPKVVLNAQG EALYFSRHPL PYQRQHPQAE WLAHHRYLRH
     IGLYAYRPDV LREITQLPPS PLELAESLEQ LRWLEAGYRI QTAETTLETI GIDTPEDVER
     ALRYLTEANG
//
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