ID   PSEI_CAMJJ              Reviewed;         343 AA.
AC   Q939J8;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Pseudaminic acid synthase;
DE            EC=2.5.1.97;
DE   AltName: Full=Pseudaminic acid biosynthesis protein I;
GN   Name=pseI; Synonyms=neuB3; OrderedLocusNames=CJJ81176_1334;
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   FUNCTION.
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 fifth step in the biosynthesis of pseudaminic
CC       acid, a sialic-acid-like sugar that is used to modify flagellin.
CC       Catalyzes the condensation of phosphoenolpyruvate with 2,4-diacetamido-
CC       2,4,6-trideoxy-beta-l-altropyranose, forming pseudaminic acid.
CC       {ECO:0000269|PubMed:16684771}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,4-diacetamido-2,4,6-trideoxy-beta-L-altrose + H2O +
CC         phosphoenolpyruvate = phosphate + pseudaminate; Xref=Rhea:RHEA:31631,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702,
CC         ChEBI:CHEBI:63282, ChEBI:CHEBI:63283; EC=2.5.1.97;
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the pseudaminic acid synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AY102622; AAK58485.1; -; Genomic_DNA.
DR   EMBL; CP000538; EAQ72890.1; -; Genomic_DNA.
DR   RefSeq; WP_002855940.1; NC_008787.1.
DR   AlphaFoldDB; Q939J8; -.
DR   SMR; Q939J8; -.
DR   STRING; 354242.CJJ81176_1334; -.
DR   EnsemblBacteria; EAQ72890; EAQ72890; CJJ81176_1334.
DR   KEGG; cjj:CJJ81176_1334; -.
DR   eggNOG; COG2089; Bacteria.
DR   HOGENOM; CLU_040465_0_1_7; -.
DR   OMA; CWDEEAV; -.
DR   Proteomes; UP000000646; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR036732; AFP_Neu5c_C_sf.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR013132; Neu5Ac_N.
DR   InterPro; IPR020030; Pseudaminic_synth_PseI.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF03102; NeuB; 1.
DR   Pfam; PF08666; SAF; 1.
DR   SMART; SM00858; SAF; 1.
DR   SUPFAM; SSF51269; SSF51269; 1.
DR   TIGRFAMs; TIGR03586; PseI; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Transferase.
FT   CHAIN           1..343
FT                   /note="Pseudaminic acid synthase"
FT                   /id="PRO_0000418935"
FT   DOMAIN          287..343
FT                   /note="AFP-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00021"
SQ   SEQUENCE   343 AA;  38659 MW;  AC81CE6266A0D7CB CRC64;
     MQIGNFNTDK KVFIIAELSA NHAGSLEMAL KSIKAAKKAG ADAIKIQTYT PDSLTLNSDK
     EDFIIKGGLW DKRKLYELYE SAKTPYEWHS QIFETAQNEG ILCFSSPFAK EDIEFLKRFD
     PIAYKIASFE ANDENFVRLI AKEKKPTIVS TGIATEEELF KICEIFKEEK NPDLIFLKCT
     SAYPTAIEDM NLKGIVSLKE KFNVEVGLSD HSFGFLAPVM AVALGARVIE KHFMLDKSIE
     SEDSKFSLDF DEFKAMVDAV RQAESALGDG KLDLDEKALK NRVFARSLYA SKDIKKGEIF
     SEENVKSVRP SFGLHPKFYQ ELLGKKASKD IEFGDALKES DFR