ID   PSEG_CAMJJ              Reviewed;         274 AA.
AC   A1W0U6; Q2M5Q1;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose hydrolase;
DE            EC=3.6.1.57;
DE   AltName: Full=Pseudaminic acid biosynthesis protein G;
GN   Name=pseG; OrderedLocusNames=CJJ81176_1329;
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: Nucleotide sugar hydrolase that catalyzes the fourth step in
CC       the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is
CC       used to modify flagellin. Mediates the removal of UDP from C-1 of UDP-
CC       2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose forming 2,4-
CC       diacetamido-2,4,6-trideoxy-beta-L-altropyranose (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altrose = 2,4-
CC         diacetamido-2,4,6-trideoxy-beta-L-altrose + H(+) + UDP;
CC         Xref=Rhea:RHEA:31803, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:63283, ChEBI:CHEBI:63417; EC=3.6.1.57;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PseG family. {ECO:0000305}.
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DR   EMBL; AY102622; ABC69288.1; -; Genomic_DNA.
DR   EMBL; CP000538; EAQ72677.1; -; Genomic_DNA.
DR   RefSeq; WP_002790573.1; NC_008787.1.
DR   AlphaFoldDB; A1W0U6; -.
DR   SMR; A1W0U6; -.
DR   STRING; 354242.CJJ81176_1329; -.
DR   EnsemblBacteria; EAQ72677; EAQ72677; CJJ81176_1329.
DR   KEGG; cjj:CJJ81176_1329; -.
DR   eggNOG; COG3980; Bacteria.
DR   HOGENOM; CLU_023406_0_0_7; -.
DR   OMA; YEVEYRY; -.
DR   Proteomes; UP000000646; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR020023; PseG.
DR   TIGRFAMs; TIGR03590; PseG; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..274
FT                   /note="UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-
FT                   altropyranose hydrolase"
FT                   /id="PRO_0000418932"
FT   ACT_SITE        17
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         15..16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         234..235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        196..274
FT                   /note="NLKKLQKFAKLHNNIRLFIDHENIAKLMNESNKLIISASSLVNEALLLKANF
FT                   KAICYVKNQESTATWLAKKGYEVEYKY -> QPK (in Ref. 1; ABC69288)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   274 AA;  31347 MW;  FDA64756A039C2AF CRC64;
     MKVLFRSDSS SQIGFGHIKR DLVLAKQYSD VSFACLPLEG SLIDEIPYPV YELDSESIYE
     LINLIKEEKF ELLIIDHYGI SVDDEKLIKL ETGVKILSFD DEIKPHHCDI LLNVNAYAKA
     SDYEGLVPFK CEVRCGFSYA LIREEFYQEA KENREKKYDF FICMGGTDIK NLSLQIASEL
     PKTKIISIAT SSSNPNLKKL QKFAKLHNNI RLFIDHENIA KLMNESNKLI ISASSLVNEA
     LLLKANFKAI CYVKNQESTA TWLAKKGYEV EYKY