ID Q59310_CLOPF Unreviewed; 694 AA.
AC Q59310;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733};
DE EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
DE Flags: Precursor;
GN Name=nanH {ECO:0000313|EMBL:CAA60796.1};
OS Clostridium perfringens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1502 {ECO:0000313|EMBL:CAA60796.1};
RN [1] {ECO:0000313|EMBL:CAA60796.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A99 {ECO:0000313|EMBL:CAA60796.1};
RX PubMed=7804004; DOI=10.1007/BF00731154;
RA Traving C., Schauer R., Roggentin P.;
RT "Gene structure of the 'large' sialidase isoenzyme from Clostridium
RT perfringens A99 and its relationship with other clostridial nanH
RT proteins.";
RL Glycoconj. J. 11:141-151(1994).
RN [2] {ECO:0000313|EMBL:CAA60796.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A99 {ECO:0000313|EMBL:CAA60796.1};
RA Zeilstra-Ryalls J.J.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007829|PDB:2BF6, ECO:0007829|PDB:2VK5}
RP X-RAY CRYSTALLOGRAPHY (0.97 ANGSTROMS) OF 243-691 IN COMPLEX WITH CALCIUM.
RX PubMed=18218621; DOI=10.1074/jbc.M710247200;
RA Newstead S.L., Potter J.A., Wilson J.C., Xu G., Chien C.H., Watts A.G.,
RA Withers S.G., Taylor G.L.;
RT "The structure of Clostridium perfringens NanI sialidase and its catalytic
RT intermediates.";
RL J. Biol. Chem. 283:9080-9088(2008).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC {ECO:0000256|ARBA:ARBA00009348}.
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DR EMBL; X87369; CAA60796.1; -; Genomic_DNA.
DR PIR; I40866; I40866.
DR PDB; 2BF6; X-ray; 0.97 A; A=243-691.
DR PDB; 2VK5; X-ray; 0.97 A; A=243-694.
DR PDB; 2VK6; X-ray; 1.50 A; A=243-694.
DR PDB; 2VK7; X-ray; 1.20 A; A/B=243-694.
DR PDBsum; 2BF6; -.
DR PDBsum; 2VK5; -.
DR PDBsum; 2VK6; -.
DR PDBsum; 2VK7; -.
DR AlphaFoldDB; Q59310; -.
DR SMR; Q59310; -.
DR CAZy; CBM40; Carbohydrate-Binding Module Family 40.
DR CAZy; GH33; Glycoside Hydrolase Family 33.
DR BRENDA; 3.2.1.18; 1503.
DR EvolutionaryTrace; Q59310; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.120.10.10; -; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR004124; Glyco_hydro_33_N.
DR InterPro; IPR011040; Sialidase.
DR InterPro; IPR026856; Sialidase_fam.
DR InterPro; IPR036278; Sialidase_sf.
DR InterPro; IPR023364; Trans_sialidase_dom3.
DR PANTHER; PTHR10628; SIALIDASE; 1.
DR PANTHER; PTHR10628:SF25; SIALIDASE-1; 1.
DR Pfam; PF13859; BNR_3; 1.
DR Pfam; PF02973; Sialidase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF50939; Sialidases; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:2BF6, ECO:0007829|PDB:2VK5};
KW Calcium {ECO:0007829|PDB:2BF6, ECO:0007829|PDB:2VK5};
KW Glycosidase {ECO:0000313|EMBL:CAA60796.1};
KW Hydrolase {ECO:0000313|EMBL:CAA60796.1};
KW Metal-binding {ECO:0007829|PDB:2BF6, ECO:0007829|PDB:2VK5};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 50..236
FT /note="Glycoside hydrolase family 33 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02973"
FT DOMAIN 268..617
FT /note="Sialidase"
FT /evidence="ECO:0000259|Pfam:PF13859"
FT BINDING 296
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:2BF6, ECO:0007829|PDB:2VK5"
FT BINDING 298
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:2BF6, ECO:0007829|PDB:2VK5"
FT BINDING 319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:2BF6, ECO:0007829|PDB:2VK5"
FT BINDING 320
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:2BF6, ECO:0007829|PDB:2VK5"
FT BINDING 515
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:2BF6, ECO:0007829|PDB:2VK5"
FT BINDING 515
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:2VK6"
FT BINDING 573
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:2BF6, ECO:0007829|PDB:2VK5"
FT BINDING 573
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:2VK6"
SQ SEQUENCE 694 AA; 77327 MW; 22D23E25A0A8DC72 CRC64;
MNYKGITLIL TAAMVISGGN YVLVKGSTLD SGKNNSGYEI KVNNSENLSS LGEYKDINLE
SSNASNITYD LEKYKNLDEG TIVVRFNSKD SKIQSLLGIS NSKTKNGYFN FYVTNSRVGF
ELRNQKNEGN TQSGTENLVH MYKDVALNDG DNTVALKIEK NKGYKLFLNG KIIKEVKDTN
TKFLNNIENL DSAFIGKTNR YGQSNEYNFK GNIGFMNIYN EPLGDDYLLS KTGETKAKEE
VLVEGAVKTE PVDLFHPGFL NSSNYRIPAL FKTKEGTLIA SIDARRHGGA DAPNNDIDTA
VRRSEDGGKT WDEGQIIMDY PDKSSVIDTT LIQDDETGRI FLLVTHFPSK YGFWNAGLGS
GFKNIDGKEY LCLYDSSGKE FTVRENVVYD KDGNKTEYTT NALGDLFKNG TKIDNINSST
APLKAKGTSY INLVYSDDDG KTWSEPQNIN FQVKKDWMKF LGIAPGRGIQ IKNGEHKGRI
VVPVYYTNEK GKQSSAVIYS DDSGKNWTIG ESPNDNRKLE NGKIINSKTL SDDAPQLTEC
QVVEMPNGQL KLFMRNLSGY LNIATSFDGG ATWDETVEKD TNVLEPYCQL SVINYSQKVD
GKDAVIFSNP NARSRSNGTV RIGLINQVGT YENGEPKYEF DWKYNKLVKP GYYAYSCLTE
LSNGNIGLLY EGTPSEEMSY IEMNLKYLES GANK
//
