ID   NEUAH_LEGPH             Reviewed;         232 AA.
AC   Q5ZXI0;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=CMP-N,N'-diacetyllegionaminic acid synthase;
DE            EC=2.7.7.82;
GN   Name=neuA; OrderedLocusNames=lpg0751;
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, AND CATALYTIC ACTIVITY.
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       conversion of N,N'-diacetyllegionaminic acid (Leg5Ac7Ac) and CTP into
CC       CMP-N,N'-diacetyllegionaminic acid (CMP-Leg5Ac7Ac).
CC       {ECO:0000269|PubMed:18275154}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CTP + N,N-diacetyllegionaminate = CMP-N,N-
CC         diacetyllegionaminate + diphosphate; Xref=Rhea:RHEA:34675,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:68669,
CC         ChEBI:CHEBI:68670; EC=2.7.7.82;
CC         Evidence={ECO:0000269|PubMed:18275154};
CC   -!- SIMILARITY: Belongs to the CMP-NeuNAc synthase family. {ECO:0000305}.
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DR   EMBL; AE017354; AAU26840.1; -; Genomic_DNA.
DR   RefSeq; WP_010946488.1; NC_002942.5.
DR   RefSeq; YP_094787.1; NC_002942.5.
DR   AlphaFoldDB; Q5ZXI0; -.
DR   SMR; Q5ZXI0; -.
DR   STRING; 272624.lpg0751; -.
DR   PaxDb; Q5ZXI0; -.
DR   EnsemblBacteria; AAU26840; AAU26840; lpg0751.
DR   GeneID; 66489938; -.
DR   KEGG; lpn:lpg0751; -.
DR   PATRIC; fig|272624.6.peg.776; -.
DR   eggNOG; COG1083; Bacteria.
DR   HOGENOM; CLU_042930_1_1_6; -.
DR   OMA; NCDEMES; -.
DR   BioCyc; MetaCyc:MON-17730; -.
DR   Proteomes; UP000000609; Chromosome.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR003329; Cytidylyl_trans.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF02348; CTP_transf_3; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..232
FT                   /note="CMP-N,N'-diacetyllegionaminic acid synthase"
FT                   /id="PRO_0000424186"
SQ   SEQUENCE   232 AA;  25764 MW;  9D3C54BC3A3589CD CRC64;
     MRILAVIPAR AGSKRLPGKN TRLLAGKPLI AHTIVAALQS SCCEEIVVST DSKQIADVAV
     QYGASVPWLR SEDLATDTSD VIHTVIDLLF KFQQMDVFFD SVLLLQPTSP FRKPETIRHA
     VEIHKVTGKS VVSVSPISLK PSWCRSIDSQ GNLVKPELFQ DLEIYCNENP IYKLNGSIYI
     ATAKQIIENK SFYSEPTKPL LLNSISESID IDTPIDWALT EKLMELNQEA LV