NEUCH_CAMJE
ID NEUCH_CAMJE Reviewed; 384 AA.
AC Q0P8T0;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=GDP/UDP-N,N'-diacetylbacillosamine 2-epimerase (hydrolyzing);
DE EC=3.2.1.184;
GN Name=legG; Synonyms=neuC2; OrderedLocusNames=Cj1328;
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, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND NOMENCLATURE.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=19282391; DOI=10.1093/glycob/cwp039;
RA Schoenhofen I.C., Vinogradov E., Whitfield D.M., Brisson J.R., Logan S.M.;
RT "The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving
RT novel GDP-linked precursors.";
RL Glycobiology 19:715-725(2009).
CC -!- FUNCTION: Involved in biosynthesis of legionaminic acid (5,7-diamino-
CC 3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonic acid)(Leg), a
CC sialic acid-like derivative that is incorporated into flagellin via O-
CC linkage to Ser/Thr. Catalyzes the conversion of GDP-N,N'-
CC diacetylbacillosamine (Bac2Ac4Ac) into 2,4-diacetamido-2,4,6-
CC trideoxymannose and GDP. It can also use UDP-N,N'-diacetylbacillosamine
CC however it generates small quantities of 2,4-diacetamido-2,4,6-
CC trideoxymannose. {ECO:0000269|PubMed:19282391}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-N,N'-diacetylbacillosamine + H2O = 2,4-diacetamido-2,4,6-
CC trideoxy-alpha-D-mannopyranose + GDP + H(+); Xref=Rhea:RHEA:46316,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:68645, ChEBI:CHEBI:86016; EC=3.2.1.184;
CC Evidence={ECO:0000269|PubMed:19282391};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UDP-N,N'-diacetylbacillosamine = 2,4-diacetamido-2,4,6-
CC trideoxy-alpha-D-mannopyranose + H(+) + UDP; Xref=Rhea:RHEA:34491,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67134, ChEBI:CHEBI:68645; EC=3.2.1.184;
CC Evidence={ECO:0000269|PubMed:19282391};
CC -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC {ECO:0000305}.
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DR EMBL; AL111168; CAL35441.1; -; Genomic_DNA.
DR PIR; E81276; E81276.
DR RefSeq; WP_002858369.1; NC_002163.1.
DR RefSeq; YP_002344717.1; NC_002163.1.
DR AlphaFoldDB; Q0P8T0; -.
DR SMR; Q0P8T0; -.
DR IntAct; Q0P8T0; 20.
DR STRING; 192222.Cj1328; -.
DR PaxDb; Q0P8T0; -.
DR PRIDE; Q0P8T0; -.
DR EnsemblBacteria; CAL35441; CAL35441; Cj1328.
DR GeneID; 905620; -.
DR KEGG; cje:Cj1328; -.
DR PATRIC; fig|192222.6.peg.1310; -.
DR eggNOG; COG0381; Bacteria.
DR HOGENOM; CLU_061127_0_0_7; -.
DR OMA; VTYHPVT; -.
DR BioCyc; MetaCyc:MON-16352; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0102224; F:GDP-2,4-diacetamido-2,4,6-trideoxy-alpha-D-glucopyranose hydrolase/2-epimerase activity; IEA:RHEA.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IDA:UniProtKB.
DR GO; GO:0102388; F:UDP-N,N'-diacetylbacillosamine 2-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:InterPro.
DR GO; GO:0044781; P:bacterial-type flagellum organization; IEA:UniProtKB-KW.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IEA:InterPro.
DR InterPro; IPR020004; UDP-GlcNAc_Epase.
DR InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
DR InterPro; IPR029767; WecB-like.
DR PANTHER; PTHR43174; PTHR43174; 1.
DR Pfam; PF02350; Epimerase_2; 1.
DR TIGRFAMs; TIGR03568; NeuC_NnaA; 1.
PE 1: Evidence at protein level;
KW Bacterial flagellum biogenesis; Hydrolase; Reference proteome.
FT CHAIN 1..384
FT /note="GDP/UDP-N,N'-diacetylbacillosamine 2-epimerase
FT (hydrolyzing)"
FT /id="PRO_0000424191"
SQ SEQUENCE 384 AA; 43766 MW; 38D71BAFEB411EB2 CRC64;
MSKRKICIVS ATRAEWYLLR NLCHEIQNDK DLSLQIIATG AHLSPEFGLT YKEIEKEFKI
TKKIPILLAN DDKISLCKSM SLAFSAFSDA FEDLKPDMVV ILGDRYEMLS VASVCLLMHI
PLVHLCGGEL TLGAIDDSIR HSISKMSHLH FVSHEIYKKR LLQLGEEEKR VFNIGSLAST
IIKNMNFLNK KDLEKALEMK LDKELYLITY HPLTLNVKNT QKEIKTLLKK LDTLKNASLI
FTKANADENG LLINEILQNY CQKNSHKAKL FDNLGSQKYL SLMKIAKAMI GNSSSGISES
PFFKTPCINI GDRQKGRLRT QNIIDSEIND LDQAFEKLES KEFKQNLKNF KNPYDNGKNP
NKIIKTCLKN VNLDTILHKN FIDL
