(data stored in ACNUC7421 zone)

SWISSPROT: KDSB_SYNFM

ID   KDSB_SYNFM              Reviewed;         250 AA.
AC   A0LE62;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 73.
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};
GN   OrderedLocusNames=Sfum_0010;
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Activates KDO (a required 8-carbon sugar) for
CC       incorporation into bacterial lipopolysaccharide in Gram-negative
CC       bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-
CC         deoxy-beta-D-manno-octulosonate + diphosphate;
CC         Xref=Rhea:RHEA:23448, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:85986, ChEBI:CHEBI:85987; EC=2.7.7.38;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00057};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-
CC       octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from
CC       3-deoxy-D-manno-octulosonate and CTP: step 1/1.
CC       {ECO:0000255|HAMAP-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}.
DR   EMBL; CP000478; ABK15714.1; -; Genomic_DNA.
DR   RefSeq; WP_011696887.1; NC_008554.1.
DR   SMR; A0LE62; -.
DR   STRING; 335543.Sfum_0010; -.
DR   EnsemblBacteria; ABK15714; ABK15714; Sfum_0010.
DR   KEGG; sfu:Sfum_0010; -.
DR   eggNOG; ENOG4105CET; Bacteria.
DR   eggNOG; COG1212; LUCA.
DR   HOGENOM; HOG000007602; -.
DR   KO; K00979; -.
DR   OMA; FMATCAK; -.
DR   OrthoDB; 1345588at2; -.
DR   BioCyc; SFUM335543:G1G7I-12-MONOMER; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00358; UER00476.
DR   Proteomes; UP000001784; 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   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   3: Inferred from homology;
DR   PRODOM; A0LE62.
DR   SWISS-2DPAGE; A0LE62.
KW   Complete proteome; Cytoplasm; Lipopolysaccharide biosynthesis;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN         1    250       3-deoxy-manno-octulosonate
FT                                cytidylyltransferase.
FT                                /FTId=PRO_1000003387.
SQ   SEQUENCE   250 AA;  27120 MW;  0C4EC8419E499C5C CRC64;
     MRIVGIIPAR YQSSRFPGKP LVDILGKPMI RHVYERSARA GCLDRLIVAT DDARIAAAVA
     GFGGEALLTR ADHASGTDRL AEAARLLELD GADIVVNIQG DEPLVNHRMI EALVEALQCD
     RHCPMATLAF PSESLQDYNN PNVVKVVLDR GLRALYFSRA PIPFVRDGAA DAPAFLKHLG
     FYAYSASFLQ TFSRLPPGRL EGLEKLEQLR ALEHGYGIRV ALSPVDTRGV DTPEDLEAVV
     PVLAQDAVGA
//

If you have problems or comments...

PBIL Back to PBIL home page