ID   NEUBH_CAMJE             Reviewed;         334 AA.
AC   Q0P8T1;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=N,N'-diacetyllegionaminic acid synthase;
DE            EC=2.5.1.101;
GN   Name=legI; Synonyms=neuB2; OrderedLocusNames=Cj1327;
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, 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 condensation of 2,4-diacetamido-
CC       2,4,6-trideoxymannose with phosphoenolpyruvate (PEP) to give N,N'-
CC       diacetyllegionaminic acid. {ECO:0000269|PubMed:19282391}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,4-diacetamido-2,4,6-trideoxy-alpha-D-mannopyranose + H2O +
CC         phosphoenolpyruvate = N,N-diacetyllegionaminate + phosphate;
CC         Xref=Rhea:RHEA:34507, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58702, ChEBI:CHEBI:68645, ChEBI:CHEBI:68669;
CC         EC=2.5.1.101; Evidence={ECO:0000269|PubMed:19282391};
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DR   EMBL; AL111168; CAL35440.1; -; Genomic_DNA.
DR   PIR; D81276; D81276.
DR   RefSeq; WP_002864265.1; NC_002163.1.
DR   RefSeq; YP_002344716.1; NC_002163.1.
DR   AlphaFoldDB; Q0P8T1; -.
DR   SMR; Q0P8T1; -.
DR   IntAct; Q0P8T1; 4.
DR   STRING; 192222.Cj1327; -.
DR   PaxDb; Q0P8T1; -.
DR   PRIDE; Q0P8T1; -.
DR   EnsemblBacteria; CAL35440; CAL35440; Cj1327.
DR   GeneID; 905619; -.
DR   KEGG; cje:Cj1327; -.
DR   PATRIC; fig|192222.6.peg.1309; -.
DR   eggNOG; COG2089; Bacteria.
DR   HOGENOM; CLU_040465_0_0_7; -.
DR   OMA; WKRMEFT; -.
DR   BioCyc; MetaCyc:MON-16353; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IDA:UniProtKB.
DR   GO; GO:0044781; P:bacterial-type flagellum organization; IEA:UniProtKB-KW.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IDA:UniProtKB.
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; IPR020007; N-AcNeuraminate_synthase.
DR   InterPro; IPR013132; Neu5Ac_N.
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; TIGR03569; NeuB_NnaB; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   1: Evidence at protein level;
KW   Bacterial flagellum biogenesis; Lyase; Reference proteome; Transferase.
FT   CHAIN           1..334
FT                   /note="N,N'-diacetyllegionaminic acid synthase"
FT                   /id="PRO_0000424189"
FT   DOMAIN          282..334
FT                   /note="AFP-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00021"
SQ   SEQUENCE   334 AA;  37091 MW;  59FA32E8EA992CFD CRC64;
     MKKTLIIAEA GVNHNGDLNL AKKLIEIAAD SGADFVKFQS FKAKNCISTK AKKAPYQLKT
     TANDESQLQM VQKLELDLKA HKELILHAKK CNIAFLSTPF DLESVDLLNE LGLKIFKIPS
     GEITNLPYLK KIAKLNKKII LSTGMANLGE IEEALNVLCK NGAKRQNITL LHCTTEYPAP
     FNEVNLKAMQ SLKDAFKLDV GYSDHTRGIH ISLAAVALGA CVIEKHFTLD KNMSGPDHKA
     SLEPQELKML CTQIRQIQKA MGDGIKKASK SEQKNINIVR KSLVAKKDIK KGEIFSEGNL
     TTKRPANGIS AMRYEEFLGK IATKNYKEDE LIRE