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Q02834 (NANH_MICVI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sialidase

EC=3.2.1.18
Alternative name(s):
Neuraminidase
Gene names
Name:nedA
OrganismMicromonospora viridifaciens
Taxonomic identifier1881 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeMicromonospora

Protein attributes

Sequence length647 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

To release sialic acids for use as carbon and energy sources for this non-pathogenic bacterium while in pathogenic microorganisms, sialidases have been suggested to be pathogenic factors.

Catalytic activity

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.

Subcellular location

Secreted.

Induction

By N-acetylneuraminic acid, colominic acid, and sialic acid.

Sequence similarities

Belongs to the glycosyl hydrolase 33 family.

Contains 5 BNR repeats.

Contains 1 F5/8 type C domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionexo-alpha-(2->3)-sialidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

exo-alpha-(2->6)-sialidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

exo-alpha-(2->8)-sialidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3737 Ref.1
Chain38 – 647610Sialidase
PRO_0000012032

Regions

Repeat102 – 11312BNR 1
Repeat175 – 18612BNR 2
Repeat239 – 25012BNR 3
Repeat287 – 29812BNR 4
Repeat348 – 35912BNR 5
Domain496 – 646151F5/8 type C

Sites

Active site921Proton acceptor By similarity
Active site2601Nucleophile Potential
Active site3701Nucleophile
Binding site681Substrate By similarity
Binding site2761Substrate By similarity

Secondary structure

.......................................................................................................... 647
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02834 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: DCC1FE5BC935B8AD

FASTA64768,830
        10         20         30         40         50         60 
MTANPYLRRL PRRRAVSFLL APALAAATVA GASPAQAIAG APVPPGGEPL YTEQDLAVNG 

        70         80         90        100        110        120 
REGFPNYRIP ALTVTPDGDL LASYDGRPTG IDAPGPNSIL QRRSTDGGRT WGEQQVVSAG 

       130        140        150        160        170        180 
QTTAPIKGFS DPSYLVDRET GTIFNFHVYS QRQGFAGSRP GTDPADPNVL HANVATSTDG 

       190        200        210        220        230        240 
GLTWSHRTIT ADITPDPGWR SRFAASGEGI QLRYGPHAGR LIQQYTIINA AGAFQAVSVY 

       250        260        270        280        290        300 
SDDHGRTWRA GEAVGVGMDE NKTVELSDGR VLLNSRDSAR SGYRKVAVST DGGHSYGPVT 

       310        320        330        340        350        360 
IDRDLPDPTN NASIIRAFPD APAGSARAKV LLFSNAASQT SRSQGTIRMS CDDGQTWPVS 

       370        380        390        400        410        420 
KVFQPGSMSY STLTALPDGT YGLLYEPGTG IRYANFNLAW LGGICAPFTI PDVALEPGQQ 

       430        440        450        460        470        480 
VTVPVAVTNQ SGIAVPKPSL QLDASPDWQV QGSVEPLMPG RQAKGQVTIT VPAGTTPGRY 

       490        500        510        520        530        540 
RVGATLRTSA GNASTTFTVT VGLLDQARMS IADVDSEETA REDGRASNVI DGNPSTFWHT 

       550        560        570        580        590        600 
EWSRADAPGY PHRISLDLGG THTISGLQYT RRQNSANEQV ADYEIYTSLN GTTWDGPVAS 

       610        620        630        640 
GRFTTSLAPQ RAVFPARDAR YIRLVALSEQ TGHKYAAVAE LEVEGQR 

« Hide

References

[1]"Cloning, expression, and characterization of the Micromonospora viridifaciens neuraminidase gene in Streptomyces lividans."
Sakurada K., Ohta T., Hasegawa M.
J. Bacteriol. 174:6896-6903(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 38-647.
Strain: ATCC 31146 / DSM 43909 / FD 23988 / JCM 3267.
[2]"The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll."
Gaskell A., Crenell S., Taylor G.
Structure 3:1197-1205(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Strain: ATCC 31146 / DSM 43909 / FD 23988 / JCM 3267.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D01045 Genomic DNA. Translation: BAA00852.1.
PIRA45244.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EURX-ray1.82A43-407[»]
1EUSX-ray2.00A43-407[»]
1EUTX-ray2.50A43-647[»]
1EUUX-ray2.50A43-647[»]
1W8NX-ray2.10A47-647[»]
1W8OX-ray1.70A47-647[»]
1WCQX-ray2.10A/B/C47-647[»]
2BERX-ray1.80A47-647[»]
2BZDX-ray2.00A/B/C47-647[»]
4J9TX-ray1.40A47-407[»]
ProteinModelPortalQ02834.
SMRQ02834. Positions 47-647.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM32. Carbohydrate-Binding Module Family 32.
GH33. Glycoside Hydrolase Family 33.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ02834.

Family and domain databases

Gene3D2.120.10.10. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 1 hit.
InterProIPR018905. A-galactase_NEW3.
IPR000421. Coagulation_fac_5/8-C_type_dom.
IPR008979. Galactose-bd-like.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR026948. Sialidase/anhydrosialidase.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
IPR006311. TAT_signal.
[Graphical view]
PANTHERPTHR10628. PTHR10628. 1 hit.
PTHR10628:SF5. PTHR10628:SF5. 1 hit.
PfamPF00754. F5_F8_type_C. 1 hit.
PF10633. NPCBM_assoc. 1 hit.
[Graphical view]
SMARTSM00231. FA58C. 1 hit.
[Graphical view]
SUPFAMSSF49785. SSF49785. 1 hit.
SSF50939. SSF50939. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS50022. FA58C_3. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ02834.

Entry information

Entry nameNANH_MICVI
AccessionPrimary (citable) accession number: Q02834
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: February 19, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries