DB code: T00208
| RLCP classification | 1.31.36210.99 : Hydrolysis | |
|---|---|---|
| CATH domain | 2.60.120.200 : Jelly Rolls | |
| 2.120.10.10 : Neuraminidase | Catalytic domain | |
| 2.60.120.200 : Jelly Rolls | ||
| E.C. | 3.2.1.18 | |
| CSA | ||
| M-CSA | ||
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 2.120.10.10 : Neuraminidase | D00173 M00310 T00064 T00065 |
| 2.60.120.200 : Jelly Rolls | S00148 D00535 D00666 M00185 S00511 T00064 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P0C6E9 |
Sialidase
|
EC
3.2.1.18
Neuraminidase NANase |
NP_231419.1
(Protein)
NC_002505.1 (DNA/RNA sequence) |
PF09264
(Sial-lect-inser)
[Graphical View] |
| KEGG enzyme name |
|---|
|
exo-alpha-sialidase
neuraminidase sialidase alpha-neuraminidase acetylneuraminidase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P0C6E9 | NANH_VIBCH | Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates. | Monomer (Probable). | Secreted. | Calcium. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00511 | N-Glycan degradation | |
| MAP00600 | Sphingolipid metabolism | |
| MAP01032 | Glycan structures - degradation |
| Compound table | |||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | ||||||||||||||||||
| KEGG-id | C00076 | C06140 | C00001 | C04730 | C06128 | C04884 | C04927 | C06139 | C00270 | C01290 | C02686 | C06135 | C04911 | C06140 | C06141 | ||||||
| E.C. | |||||||||||||||||||||
| Compound | Calcium | GT1b | H2O | GM3 | N-Acetylneuraminyl-galactosylceramide | N-Acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide | N-Acetylneuraminyl-D-galactosyl-N-acetyl-D-galactosaminyl-(N- acetylneuraminyl)-D-galactosyl-D-glucosylceramide | GQ1 | N-Acetylneuraminate | beta-D-Galactosyl-1,4-beta-D-glucosylceramide | Galactosylceramide | GA2 | D-Galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide | GT1b | GD1b | ||||||
| Type | divalent metal (Ca2+, Mg2+) | amide group,carbohydrate,carboxyl group,lipid,polysaccharide | H2O | amide group,carbohydrate,carboxyl group,lipid,polysaccharide | amide group,carbohydrate,carboxyl group,lipid,polysaccharide | amide group,carbohydrate,carboxyl group,lipid,polysaccharide | amide group,carbohydrate,carboxyl group,lipid,polysaccharide | amide group,carbohydrate,carboxyl group,lipid,polysaccharide | amide group,carbohydrate,carboxyl group | amide group,carbohydrate,lipid,polysaccharide | amide group,carbohydrate,lipid | amide group,carbohydrate,lipid,polysaccharide | amide group,carbohydrate,carboxyl group,lipid,polysaccharide | amide group,carbohydrate,carboxyl group,lipid,polysaccharide | amide group,carbohydrate,carboxyl group,lipid,polysaccharide | ||||||
| ChEBI |
29108 29108 |
15377 15377 |
17012 17012 |
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| PubChem |
271 271 |
22247451 962 22247451 962 |
439197 439197 |
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| 1kitA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1w0oA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1w0pA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1kitA02 |
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Bound:2x_CA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1w0oA02 |
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Bound:2x_CA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:DAN | |
| 1w0pA02 |
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Bound:2x_CA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1kitA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1w0oA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1w0pA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| See T00065 | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1kitA01 |
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| 1w0oA01 |
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| 1w0pA01 |
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| 1kitA02 |
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ASP 250;GLU 619;TYR 740 | ALA 253;ASN 256;ASP 289;THR 313(Calcium-1);PRO 548;ASP 621;ASP 682;ALA 683(Calcium-2) | |||
| 1w0oA02 |
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ASP 250;GLU 619;TYR 740 | ALA 253;ASN 256;ASP 289;THR 313(Calcium-1);PRO 548;ASP 621;ASP 682;ALA 683(Calcium-2) | |||
| 1w0pA02 |
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ASP 250;GLU 619;TYR 740 | ALA 253;ASN 256;ASP 289;THR 313(Calcium-1);PRO 548;ASP 621;ASP 682;ALA 683(Calcium-2) | |||
| 1kitA03 |
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| 1w0oA03 |
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| 1w0pA03 |
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| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[4]
|
p.539-541 | |
|
[9]
|
Scheme 1, p.348 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1797392 |
| Journal | Carbohydr Res |
| Year | 1991 |
| Volume | 216 |
| Pages | 61-6 |
| Authors | Schreiner E, Zbiral E, Kleineidam RG, Schauer R |
| Title | 2,3-Didehydro-2-deoxysialic acids structurally varied at C-5 and their behaviour towards the sialidase from Vibrio cholerae. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments |
CHARACTERIZATION, |
| Medline ID | 92389334 |
| PubMed ID | 1518058 |
| Journal | J Mol Biol |
| Year | 1992 |
| Volume | 226 |
| Pages | 1287-90 |
| Authors | Taylor G, Vimr E, Garman E, Laver G |
| Title |
Purification, |
| Related PDB | |
| Related UniProtKB | P37060 |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8379920 |
| Journal | Biochem J |
| Year | 1993 |
| Volume | 294 |
| Pages | 653-6 |
| Authors | Guo X, Sinnott ML |
| Title | A kinetic-isotope-effect study of catalysis by Vibrio cholerae neuraminidase. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). |
| Medline ID | 95006320 |
| PubMed ID | 7922030 |
| Journal | Structure |
| Year | 1994 |
| Volume | 2 |
| Pages | 535-44 |
| Authors | Crennell S, Garman E, Laver G, Vimr E, Taylor G |
| Title | Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain. |
| Related PDB | 1kit |
| Related UniProtKB | P37060 |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8994884 |
| Journal | Curr Opin Struct Biol |
| Year | 1996 |
| Volume | 6 |
| Pages | 830-7 |
| Authors | Taylor G |
| Title |
Sialidases: structures, |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10822584 |
| Journal | Org Lett |
| Year | 1999 |
| Volume | 1 |
| Pages | 443-6 |
| Authors | Wilson JC, Kiefel MJ, Angus DI, von Itzstein M |
| Title | Investigation of the stability of thiosialosides toward hydrolysis by sialidases using NMR spectroscopy. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12797770 |
| Journal | J Am Chem Soc |
| Year | 2003 |
| Volume | 125 |
| Pages | 7154-5 |
| Authors | Thobhani S, Ember B, Siriwardena A, Boons GJ |
| Title | Multivalency and the mode of action of bacterial sialidases. |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 15226294 |
| Journal | J Biol Chem |
| Year | 2004 |
| Volume | 279 |
| Pages | 40819-26 |
| Authors | Moustafa I, Connaris H, Taylor M, Zaitsev V, Wilson JC, Kiefel MJ, von Itzstein M, Taylor G |
| Title | Sialic acid recognition by Vibrio cholerae neuraminidase. |
| Related PDB | 1w0o 1w0p |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15211517 |
| Journal | Proteins |
| Year | 2004 |
| Volume | 56 |
| Pages | 346-53 |
| Authors | Haselhorst T, Wilson JC, Thomson RJ, McAtamney S, Menting JG, Coppel RL, von Itzstein M |
| Title | Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experiments to probe the binding of N-acetylneuraminic acid and derivatives to Vibrio cholerae sialidase. |
| Related PDB | |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 16128567 |
| Journal | Biochemistry |
| Year | 2005 |
| Volume | 44 |
| Pages | 11669-75 |
| Authors | Hinou H, Kurogochi M, Shimizu H, Nishimura S |
| Title | Characterization of Vibrio cholerae neuraminidase by a novel mechanism-based fluorescent labeling reagent. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme belongs to the glycosidase family-33.
This enzyme is composed of three domains. Although this enzyme binds two calcium ions, Since the active site of this enzyme is conserved and the same as that of its homologous enzyme, Asp250 acts as a general acid-base, |
| Created | Updated |
|---|---|
| 2006-12-06 | 2009-02-26 |