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Database: UniProt
Entry: B2ULW9_AKKM8
LinkDB: B2ULW9_AKKM8
Original site: B2ULW9_AKKM8 
ID   B2ULW9_AKKM8            Unreviewed;       249 AA.
AC   B2ULW9;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 91.
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   OrderedLocusNames=Amuc_0169 {ECO:0000313|EMBL:ACD04013.1};
OS   Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS   81048 / CCUG 64013 / CIP 107961 / Muc).
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC   Akkermansiaceae; Akkermansia.
OX   NCBI_TaxID=349741 {ECO:0000313|EMBL:ACD04013.1, ECO:0000313|Proteomes:UP000001031};
RN   [1] {ECO:0000313|Proteomes:UP000001031}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013
RC   / CIP 107961 / Muc {ECO:0000313|Proteomes:UP000001031};
RX   PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA   van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA   Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT   "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT   degrader, and its use in exploring intestinal metagenomes.";
RL   PLoS ONE 6:E16876-E16876(2011).
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: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000256|HAMAP-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; CP001071; ACD04013.1; -; Genomic_DNA.
DR   RefSeq; WP_012419228.1; NZ_CP071807.1.
DR   AlphaFoldDB; B2ULW9; -.
DR   SMR; B2ULW9; -.
DR   STRING; 349741.Amuc_0169; -.
DR   PaxDb; 349741-Amuc_0169; -.
DR   KEGG; amu:Amuc_0169; -.
DR   eggNOG; COG1212; Bacteria.
DR   HOGENOM; CLU_065038_0_1_0; -.
DR   OrthoDB; 9815559at2; -.
DR   BioCyc; AMUC349741:G1GBX-195-MONOMER; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00358; UER00476.
DR   Proteomes; UP000001031; 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:UP000001031};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00057}.
SQ   SEQUENCE   249 AA;  27491 MW;  BFD316F9E6E04E6D CRC64;
     MAADTSHHII GLIPSRWGSS RFPGKPLHPI AGKPLVQHVW ERVCRCSRLD AIAIATDDQR
     IFDAAVSFGA RAIMTSPDHP SGSDRLAEAV RSFPAATHVV NIQGDEPLID PALIDRLAEA
     LVSDEALSMA TVACPISTRE DLDNPNIVKV ALARNGDALY FSRSVIPYAR HPRVAPPLRH
     LGIYAYRRDF LENYVRWAPT PLEQTESLEQ LRALENGARI RVILTDHVSV GVDTPEQAEQ
     VEQILLNIH
//
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