NANH_BACFR
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 03-AUG-2022, entry version 126.
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; Bacteroidetes; 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 EnsemblBacteria; BAD48476; BAD48476; BF1729.
DR GeneID; 66329454; -.
DR KEGG; bfr:BF1729; -.
DR PATRIC; fig|295405.11.peg.1678; -.
DR HOGENOM; CLU_024620_0_0_10; -.
DR OMA; RAWWSSH; -.
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 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; PTHR10628; 1.
DR Pfam; PF13859; BNR_3; 1.
DR Pfam; PF14873; BNR_assoc_N; 1.
DR PRINTS; PR01803; TCSIALIDASE.
DR SUPFAM; SSF50939; SSF50939; 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
