ID   NEUBH_LEGPH             Reviewed;         356 AA.
AC   Q5ZXH9;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=N,N'-diacetyllegionaminic acid synthase;
DE            EC=2.5.1.101;
GN   Name=neuB; OrderedLocusNames=lpg0752;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(2004).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=18275154; DOI=10.1021/bi702364s;
RA   Glaze P.A., Watson D.C., Young N.M., Tanner M.E.;
RT   "Biosynthesis of CMP-N,N'-diacetyllegionaminic acid from UDP-N,N'-
RT   diacetylbacillosamine in Legionella pneumophila.";
RL   Biochemistry 47:3272-3282(2008).
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 virulence-
CC       associated cell surface glycoconjugates such as lipopolysaccharide
CC       (LPS) which could be a key determinant in the ability of L.pneumophila
CC       to inhibit the fusion of phagosomes with lysosomes. LPS contains a
CC       majority alpha2,4-linked homomer of legionaminic acid. Catalyzes the
CC       condensation of 2,4-diacetamido-2,4,6-trideoxymannose with
CC       phosphoenolpyruvate (PEP) to give N,N'-diacetyllegionaminic acid.
CC       {ECO:0000269|PubMed:18275154}.
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:18275154};
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DR   EMBL; AE017354; AAU26841.1; -; Genomic_DNA.
DR   RefSeq; YP_094788.1; NC_002942.5.
DR   AlphaFoldDB; Q5ZXH9; -.
DR   SMR; Q5ZXH9; -.
DR   STRING; 272624.lpg0752; -.
DR   PaxDb; Q5ZXH9; -.
DR   PRIDE; Q5ZXH9; -.
DR   EnsemblBacteria; AAU26841; AAU26841; lpg0752.
DR   KEGG; lpn:lpg0752; -.
DR   PATRIC; fig|272624.6.peg.777; -.
DR   eggNOG; COG2089; Bacteria.
DR   HOGENOM; CLU_040465_0_0_6; -.
DR   OMA; YRHRVEF; -.
DR   BioCyc; MetaCyc:MON-17729; -.
DR   Proteomes; UP000000609; 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: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   Lyase; Reference proteome; Transferase; Virulence.
FT   CHAIN           1..356
FT                   /note="N,N'-diacetyllegionaminic acid synthase"
FT                   /id="PRO_0000424188"
FT   DOMAIN          299..356
FT                   /note="AFP-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00021"
SQ   SEQUENCE   356 AA;  38991 MW;  CE41487F543A5414 CRC64;
     MGSNRKINGI KPRGSSMTCF IIAEAGVNHN GDLQLAKELV YAAKESGADA VKFQTFKADT
     LVNKTVEKAE YQKNNAPESS TQYEMLKALE LSEEDHYLLS ELANSLGIEF MSTGFDEQSI
     DFLISLGVKR LKIPSGEITN VPYLQHCASK KLPLIISTGM CDLQEVRVAI DTVKPYYGNS
     LSDYLVLLHC TSNYPASYQD VNLKAMQTLA DEFQLPVGYS DHTLGILVPT LAVGMGACVI
     EKHFTMDKSL PGPDHLASMD PEEMKNLVQS IRDAETVLGS GEKKPSDNEL PIRALVRRSI
     TLRRDLVKGA QISKEDLILL RPGTGIAPSE ISNIVGSRLS MNLSAGTTLL WEHIEA