PSEB_CAMJJ
ID PSEB_CAMJJ Reviewed; 334 AA.
AC Q5QKR8;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=UDP-N-acetylglucosamine 4,6-dehydratase (inverting);
DE EC=4.2.1.115;
DE AltName: Full=Pseudaminic acid biosynthesis protein B;
DE AltName: Full=UDP-GlcNAc-inverting 4,6-dehydratase;
GN Name=pseB; Synonyms=flmA; OrderedLocusNames=CJJ81176_1310;
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 [GENOMIC DNA].
RC STRAIN=81-176;
RX PubMed=16861657; DOI=10.1128/iai.00210-06;
RA Hofreuter D., Tsai J., Watson R.O., Novik V., Altman B., Benitez M.,
RA Clark C., Perbost C., Jarvie T., Du L., Galan J.E.;
RT "Unique features of a highly pathogenic Campylobacter jejuni strain.";
RL Infect. Immun. 74:4694-4707(2006).
RN [3]
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 [4]
RP PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=81-176;
RX PubMed=14617187; DOI=10.1046/j.1365-2958.2003.03725.x;
RA Goon S., Kelly J.F., Logan S.M., Ewing C.P., Guerry P.;
RT "Pseudaminic acid, the major modification on Campylobacter flagellin, is
RT synthesized via the Cj1293 gene.";
RL Mol. Microbiol. 50:659-671(2003).
RN [5]
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 first step in the biosynthesis of pseudaminic
CC acid, a sialic-acid-like sugar that is used to modify flagellin. Has
CC both C6 dehydratase and C5 epimerase activities that result in the
CC production of both UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-
CC hexulose and UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose.
CC {ECO:0000269|PubMed:16684771}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-N-acetyl-alpha-D-glucosamine = H2O + UDP-2-acetamido-2,6-
CC dideoxy-beta-L-arabino-hex-4-ulose; Xref=Rhea:RHEA:26111,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57705, ChEBI:CHEBI:60101;
CC EC=4.2.1.115;
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells are non-motile and non-flagellated and
CC accumulate unglycosylated flagellin intracellularly.
CC {ECO:0000269|PubMed:14617187}.
CC -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC {ECO:0000305}.
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DR EMBL; AY102622; AAP12668.1; -; Genomic_DNA.
DR EMBL; DQ493920; ABF83716.1; -; Genomic_DNA.
DR EMBL; CP000538; EAQ72897.1; -; Genomic_DNA.
DR RefSeq; WP_002869093.1; NC_008787.1.
DR AlphaFoldDB; Q5QKR8; -.
DR SMR; Q5QKR8; -.
DR STRING; 354242.CJJ81176_1310; -.
DR EnsemblBacteria; EAQ72897; EAQ72897; CJJ81176_1310.
DR KEGG; cjj:CJJ81176_1310; -.
DR eggNOG; COG1086; Bacteria.
DR HOGENOM; CLU_013560_4_1_7; -.
DR OMA; HEVMIPK; -.
DR Proteomes; UP000000646; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR CDD; cd05237; UDP_invert_4-6DH_SDR_e; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003869; Polysac_CapD-like.
DR InterPro; IPR020025; PseB.
DR Pfam; PF02719; Polysacc_synt_2; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03589; PseB; 1.
PE 3: Inferred from homology;
KW Lyase; NADP; Nucleotide-binding.
FT CHAIN 1..334
FT /note="UDP-N-acetylglucosamine 4,6-dehydratase (inverting)"
FT /id="PRO_0000418956"
FT ACT_SITE 127
FT /evidence="ECO:0000250"
FT BINDING 13..16
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 37..42
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 61..62
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 123..124
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168..172
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 334 AA; 37360 MW; 76899A2106071288 CRC64;
MFNGKNILIT GGTGSFGKTY TKVLLENYKP NKIIIYSRDE LKQFEMSSIF NSNCMRYFIG
DVRDKERLSV AMRDVDFVIH AAAMKHVPVA EYNPMECIKT NIHGAQNVID ACFENGVKKC
IALSTDKACN PVNLYGATKL ASDKLFVAAN NIAGNKQTRF SVTRYGNVVG SRGSVVPFFK
KLIAQGSKEL PITDTRMTRF WISLEDGVKF VLSNFERMHG GEIFIPKIPS MKITNLAHAL
APNLSHKIIG IRAGEKLHEI MISSDDSHLT YEFENYYAIS PSIKLVDQES DFSINALGEK
GQKVKDGFSY SSDNNPQWAS EKELLDIINH TEGF
