ID   NEUCH_LEGPH             Reviewed;         377 AA.
AC   Q5ZXH8;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=UDP-N,N'-diacetylbacillosamine 2-epimerase (hydrolyzing);
DE            EC=3.2.1.184;
GN   OrderedLocusNames=lpg0753;
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, BIOPHYSICOCHEMICAL PROPERTIES, AND REACTION
RP   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       conversion of UDP-N,N'-diacetylbacillosamine (Bac2Ac4Ac) into 2,4-
CC       diacetamido-2,4,6-trideoxymannose and UDP.
CC       {ECO:0000269|PubMed:18275154}.
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:18275154};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=36.5 uM for UDP-N,N'-diacetylbacillosamine (at pH 7.5 and 37
CC         degrees Celsius) {ECO:0000269|PubMed:18275154};
CC         Note=kcat is 59.1 sec(-1) for UDP-N,N'-diacetylbacillosamine (at pH
CC         7.5 and 37 degrees Celsius).;
CC   -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC       {ECO:0000305}.
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DR   EMBL; AE017354; AAU26842.1; -; Genomic_DNA.
DR   RefSeq; WP_010946490.1; NC_002942.5.
DR   RefSeq; YP_094789.1; NC_002942.5.
DR   AlphaFoldDB; Q5ZXH8; -.
DR   SMR; Q5ZXH8; -.
DR   STRING; 272624.lpg0753; -.
DR   PaxDb; Q5ZXH8; -.
DR   EnsemblBacteria; AAU26842; AAU26842; lpg0753.
DR   GeneID; 66489940; -.
DR   KEGG; lpn:lpg0753; -.
DR   PATRIC; fig|272624.6.peg.778; -.
DR   eggNOG; COG0381; Bacteria.
DR   HOGENOM; CLU_061127_0_0_6; -.
DR   OMA; VTYHPVT; -.
DR   BioCyc; MetaCyc:MON-17728; -.
DR   Proteomes; UP000000609; Chromosome.
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: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   Hydrolase; Reference proteome; Virulence.
FT   CHAIN           1..377
FT                   /note="UDP-N,N'-diacetylbacillosamine 2-epimerase
FT                   (hydrolyzing)"
FT                   /id="PRO_0000424190"
SQ   SEQUENCE   377 AA;  42110 MW;  4CA0C3C19D80014B CRC64;
     MIRKIIYVTG TRADYGLMRE VLKRLHQSED IDLSICVTGM HLDALYGNTV NEIKADQFSI
     CGIIPVDLAN AQHSSMAKAI GHELLGFTEV FESETPDVVL LLGDRGEMLA AAIAAIHLNI
     PVVHLHGGER SGTVDEMVRH AISKLSHYHF VATEASKQRL IRMGEKEETI FQVGAPGLDE
     IMQYKTSTRD VFNQRYGFDP DKKICLLIYH PVVQEVDSIK IQFQSVIQAA LATNLQIICL
     EPNSDTGGHL IREVIQEYID HPDVRIIKHL HRPEFIDCLA NSDVMLGNSS SGIIEAASFN
     LNVVNVGSRQ NLRERSDNVI DVDVTYDAIL TGLREALNKP KIKYSNCYGD GKTSERCYQL
     LKTIPLHSQI LNKCNAY