ID   PSEF_CAMJJ              Reviewed;         232 AA.
AC   Q2M5Q2;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Pseudaminic acid cytidylyltransferase;
DE            EC=2.7.7.81;
DE   AltName: Full=Pseudaminic acid biosynthesis protein F;
GN   Name=pseF; Synonyms=neuA; OrderedLocusNames=CJJ81176_1328;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=81-176;
RX   PubMed=11461915; DOI=10.1074/jbc.m104529200;
RA   Thibault P., Logan S.M., Kelly J.F., Brisson J.-R., Ewing C.P., Trust T.J.,
RA   Guerry P.;
RT   "Identification of the carbohydrate moieties and glycosylation motifs in
RT   Campylobacter jejuni flagellin.";
RL   J. Biol. Chem. 276:34862-34870(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   IDENTIFICATION.
RC   STRAIN=81-176;
RX   PubMed=16684771; DOI=10.1074/jbc.m603777200;
RA   McNally D.J., Hui J.P., Aubry A.J., Mui K.K., Guerry P., Brisson J.R.,
RA   Logan S.M., Soo E.C.;
RT   "Functional characterization of the flagellar glycosylation locus in
RT   Campylobacter jejuni 81-176 using a focused metabolomics approach.";
RL   J. Biol. Chem. 281:18489-18498(2006).
CC   -!- FUNCTION: Catalyzes the final step in the biosynthesis of pseudaminic
CC       acid, a sialic-acid-like sugar that is used to modify flagellin.
CC       Mediates the activation of pseudaminic acid with CMP by forming CMP-
CC       pseudaminic acid (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CTP + pseudaminate = CMP-pseudaminate + diphosphate;
CC         Xref=Rhea:RHEA:32083, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:63282, ChEBI:CHEBI:63680; EC=2.7.7.81;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the CMP-NeuNAc synthase family. {ECO:0000305}.
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DR   EMBL; AY102622; ABC69287.1; -; Genomic_DNA.
DR   EMBL; CP000538; EAQ72623.1; -; Genomic_DNA.
DR   RefSeq; WP_002869384.1; NC_008787.1.
DR   AlphaFoldDB; Q2M5Q2; -.
DR   SMR; Q2M5Q2; -.
DR   STRING; 354242.CJJ81176_1328; -.
DR   EnsemblBacteria; EAQ72623; EAQ72623; CJJ81176_1328.
DR   KEGG; cjj:CJJ81176_1328; -.
DR   eggNOG; COG1083; Bacteria.
DR   HOGENOM; CLU_042930_1_0_7; -.
DR   OMA; AYHMKEL; -.
DR   Proteomes; UP000000646; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR003329; Cytidylyl_trans.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR020039; PseF.
DR   Pfam; PF02348; CTP_transf_3; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR03584; PseF; 1.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..232
FT                   /note="Pseudaminic acid cytidylyltransferase"
FT                   /id="PRO_0000418938"
SQ   SEQUENCE   232 AA;  26614 MW;  B50EBF684397E065 CRC64;
     MKNLCIIPAR GGSKRIPRKN IIDFLGKPLI AYSIENALNS GIFDEIVLSS DDEEIIEVAL
     KYGAKAPFVR DKNLSDDYAS STAAVQNAIE ILQSQNQIYD HVCCLYATAP LLNKNILKQA
     YEKFIQNQSK FLFAATEFEY PIQRAFYLNE NNQVYMFDEK HYKSRSQDLT KAYHDAGAFY
     FGTSKAWLEE DFIFKPHSSV FVLPRNLVCD IDTMQDLEFA KILYKVNHES AF