ID   NANH_BACFR              Reviewed;         544 AA.
AC   P31206; Q45145; Q64VK0;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=Sialidase;
DE            EC=3.2.1.18;
DE   AltName: Full=Neuraminidase;
DE   Flags: Precursor;
GN   Name=nanH; OrderedLocusNames=BF1729;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=8093075; DOI=10.1006/bbrc.1994.2269;
RA   Akimoto S., Ono T., Tsutsui H., Kinouchi T., Kataoka K., Ohnishi Y.;
RT   "Complete sequence of the Bacteroides fragilis YCH46 neuraminidase-encoding
RT   gene.";
RL   Biochem. Biophys. Res. Commun. 203:914-921(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YCH46;
RA   Nakayama H., Kuwahara T., Iwasa T., Okamoto S., Tsuchihashi Y.,
RA   Nakanishi K., Kataoka K., Arimochi H., Ohnishi Y.;
RT   "Characterization of a gene cluster for degradation of sialoglycoconjugates
RT   in Bacteroides fragilis strain YCH46.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 235-500.
RC   STRAIN=TAL2480;
RX   PubMed=2158974; DOI=10.1128/jb.172.5.2594-2600.1990;
RA   Russo T.A., Thompson J.S., Godoy V.G., Malamy M.H.;
RT   "Cloning and expression of the Bacteroides fragilis TAL2480 neuraminidase
RT   gene, nanH, in Escherichia coli.";
RL   J. Bacteriol. 172:2594-2600(1990).
CC   -!- FUNCTION: Sialidases have been suggested to be pathogenic factors in
CC       microbial infections.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-
CC         (2->8)- glycosidic linkages of terminal sialic acid residues in
CC         oligosaccharides, glycoproteins, glycolipids, colominic acid and
CC         synthetic substrates.; EC=3.2.1.18;
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. {ECO:0000305}.
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DR   EMBL; D28493; BAA05853.1; -; Genomic_DNA.
DR   EMBL; AB102772; BAC56895.2; -; Genomic_DNA.
DR   EMBL; AP006841; BAD48476.1; -; Genomic_DNA.
DR   EMBL; M31663; AAA22912.1; -; Genomic_DNA.
DR   PIR; JC2500; JC2500.
DR   RefSeq; WP_005786655.1; NC_006347.1.
DR   RefSeq; YP_099010.1; NC_006347.1.
DR   AlphaFoldDB; P31206; -.
DR   SMR; P31206; -.
DR   STRING; 295405.BF1729; -.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   GeneID; 66329454; -.
DR   KEGG; bfr:BF1729; -.
DR   PATRIC; fig|295405.11.peg.1678; -.
DR   HOGENOM; CLU_024620_0_0_10; -.
DR   OrthoDB; 7294637at2; -.
DR   Proteomes; UP000002197; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   Gene3D; 2.120.10.10; -; 1.
DR   Gene3D; 2.60.40.1290; -; 1.
DR   InterPro; IPR011040; Sialidase.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR029456; Sialidase_N.
DR   InterPro; IPR036278; Sialidase_sf.
DR   InterPro; IPR008377; Sialidase_trypan.
DR   PANTHER; PTHR10628; SIALIDASE; 1.
DR   PANTHER; PTHR10628:SF19; SIALIDASE; 1.
DR   Pfam; PF13859; BNR_3; 1.
DR   Pfam; PF14873; BNR_assoc_N; 1.
DR   PRINTS; PR01803; TCSIALIDASE.
DR   SUPFAM; SSF50939; Sialidases; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Periplasm; Repeat; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..544
FT                   /note="Sialidase"
FT                   /id="PRO_0000012029"
FT   REPEAT          239..250
FT                   /note="BNR 1"
FT   REPEAT          318..329
FT                   /note="BNR 2"
FT   REPEAT          378..389
FT                   /note="BNR 3"
FT   REPEAT          425..436
FT                   /note="BNR 4"
FT   REPEAT          485..496
FT                   /note="BNR 5"
FT   ACT_SITE        399
FT                   /evidence="ECO:0000255"
FT   BINDING         415
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         479
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        197
FT                   /note="D -> A (in Ref. 1; BAA05853)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        405
FT                   /note="V -> A (in Ref. 4; AAA22912)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   544 AA;  59556 MW;  6D1D185AB15FA822 CRC64;
     MKKAVILFSL FCFLCAIPVV QAADTIFVRE TRIPILIERQ DNVLFYLRLD AKESQTLNDV
     VLNLGEGVNL SEIQSIKLYY GGTEALQDSG KKRFAPVGYI SSNTPGKTLA ANPSYSIKKS
     EVTNPGNQVV LKGDQKLFPG INYFWISLQM KPGTSLTSKV TADIASITLD GKKALLDVVS
     ENGIEHRMGV GVRHAGDDNS AAFRIPGLVT TNKGTLLGVY DVRYNSSVDL QEHVDVGLSR
     STDGGKTWEK MRLPLAFGEF GGLPAGQNGV GDPSILVDTK TNNVWVVAAW THGMGNQRAW
     WSSHPGMDMN HTAQLVLAKS TDDGKTWSAP INITEQVKDP SWYFLLQGPG RGITMSDGTL
     VFPTQFIDST RVPNAGIMYS KDGGKNWKMH NYARTNTTEA QVAEVEPGVL MLNMRDNRGG
     SRAVAITKDL GKTWTEHESS RKALPESVCM ASLISVKAKD NVLGKDLLIF SNPNTTKGRY
     NTTIKISLDG GVTWSPEHQL LLDEGNNWGY SCLSMIDKET IGILYESSVA HMTFQAVKLK
     DIIK
//