PSEB_CAMJE
ID PSEB_CAMJE Reviewed; 334 AA.
AC Q0P8W4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
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; OrderedLocusNames=Cj1293;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=16286454; DOI=10.1074/jbc.m511021200;
RA Schoenhofen I.C., McNally D.J., Vinogradov E., Whitfield D., Young N.M.,
RA Dick S., Wakarchuk W.W., Brisson J.R., Logan S.M.;
RT "Functional characterization of dehydratase/aminotransferase pairs from
RT Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid
RT and bacillosamine biosynthetic pathways.";
RL J. Biol. Chem. 281:723-732(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:16286454}.
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; Evidence={ECO:0000269|PubMed:16286454};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC {ECO:0000305}.
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DR EMBL; AL111168; CAL35407.1; -; Genomic_DNA.
DR PIR; B81272; B81272.
DR RefSeq; WP_002858028.1; NC_002163.1.
DR RefSeq; YP_002344683.1; NC_002163.1.
DR AlphaFoldDB; Q0P8W4; -.
DR SMR; Q0P8W4; -.
DR IntAct; Q0P8W4; 7.
DR STRING; 192222.Cj1293; -.
DR PaxDb; Q0P8W4; -.
DR PRIDE; Q0P8W4; -.
DR EnsemblBacteria; CAL35407; CAL35407; Cj1293.
DR GeneID; 905585; -.
DR KEGG; cje:Cj1293; -.
DR PATRIC; fig|192222.6.peg.1275; -.
DR eggNOG; COG1086; Bacteria.
DR HOGENOM; CLU_013560_4_1_7; -.
DR OMA; HEVMIPK; -.
DR Proteomes; UP000000799; 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 1: Evidence at protein level;
KW Lyase; NADP; Nucleotide-binding; Reference proteome.
FT CHAIN 1..334
FT /note="UDP-N-acetylglucosamine 4,6-dehydratase (inverting)"
FT /id="PRO_0000418955"
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; 37372 MW; 3496887F29A79235 CRC64;
MFNKKNILIT GGTGSFGKTY TKVLLENYKP NKIIIYSRDE LKQFEMASVF NAPCMRYFIG
DVRDKERLSA AMRDVDFVIH AAAMKHVPIA EYNPMECIKT NIHGAQNVID ACFENGVKKC
IALSTDKACN PVNLYGATKL ASDKLFVAAN NIAGNKQTRF GVTRYGNVVG SRGSVVPFFK
KLISEGAKEL PITDTRMTRF WISLEDGVKF VLSNFERMHG GEIFIPKIPS MKITDLAHAL
APNLSHKIIG IRAGEKLHEI MISSDDSHLT YEFENYYAIS PSIKFVDKDN DFSINALGEK
GQKVKDGFSY SSDNNPLWAS EKELLEIINH TEGF
