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Protein

Sialidase

Gene
N/A
Organism
Clostridium sordellii
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Sialidases have been suggested to be pathogenic factors in microbial infections.

Catalytic activityi

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei55SubstrateBy similarity1
Active sitei80Proton acceptorBy similarity1
Binding sitei263SubstrateSequence analysis1
Active sitei365NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH33. Glycoside Hydrolase Family 33.

Names & Taxonomyi

Protein namesi
Recommended name:
Sialidase (EC:3.2.1.18)
Alternative name(s):
Neuraminidase
OrganismiClostridium sordellii
Taxonomic identifieri1505 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptostreptococcaceaePaeniclostridium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27PROSITE-ProRule annotation1 PublicationAdd BLAST27
ChainiPRO_000001203028 – 404SialidaseAdd BLAST377

Post-translational modificationi

It is possible that the sialidase is cleaved in front of a cysteine within the leader peptide, forming a glyceride thioether bond which links the protein to the membrane. A second proteolytic cleavage releases the mature extracellular protein.

Structurei

3D structure databases

ProteinModelPortaliP15698.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati89 – 100BNR 1Add BLAST12
Repeati158 – 169BNR 2Add BLAST12
Repeati226 – 237BNR 3Add BLAST12
Repeati273 – 284BNR 4Add BLAST12

Sequence similaritiesi

Belongs to the glycosyl hydrolase 33 family.Curated
Contains 4 BNR repeats.Curated

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR026856. Sialidase_fam.
IPR008377. Sialidase_trypan.
IPR011040. Sialidases.
[Graphical view]
PANTHERiPTHR10628. PTHR10628. 1 hit.
PfamiPF13859. BNR_3. 1 hit.
[Graphical view]
PRINTSiPR01803. TCSIALIDASE.
SUPFAMiSSF50939. SSF50939. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15698-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKFIKILKV LSMAIVLSAC NINGIFASNL NTTNEPQKTT VFNKNDNTWN
60 70 80 90 100
AQYFRIPSLQ TLADGTMLAF SDIRYNGAED HAYIDIGAAK STDNGQTWDY
110 120 130 140 150
KTVMENDRID STFSRVMDST TVVTDTGRII LIAGSWNKNG NWASSTTSLR
160 170 180 190 200
SDWSVQMVYS DDNGETWSDK VDLTTNKARI KNQPSNTIGW LAGVGSGIVM
210 220 230 240 250
SDGTIVMPIQ IALRENNANN YYSSVIYSKD NGETWTMGNK VPDPKTSENM
260 270 280 290 300
VIELDGALIM SSRNDGKNYR ASYISYDMGS TWEVYDPLHN KISTGNGSGC
310 320 330 340 350
QGSFIKVTAK DGHRLGFISA PKNTKGGYVR DNITVYMIDF DDLSKGIREL
360 370 380 390 400
CSPYPEDGNS SGGGYSCLSF NDGKLSILYE ANGNIEYKDL TDYYLSIENN

KKLK
Length:404
Mass (Da):44,729
Last modified:April 1, 1990 - v1
Checksum:i525B9DA90083AA6A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31584 Genomic DNA. Translation: AAA23280.1.
PIRiA37234.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31584 Genomic DNA. Translation: AAA23280.1.
PIRiA37234.

3D structure databases

ProteinModelPortaliP15698.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH33. Glycoside Hydrolase Family 33.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR026856. Sialidase_fam.
IPR008377. Sialidase_trypan.
IPR011040. Sialidases.
[Graphical view]
PANTHERiPTHR10628. PTHR10628. 1 hit.
PfamiPF13859. BNR_3. 1 hit.
[Graphical view]
PRINTSiPR01803. TCSIALIDASE.
SUPFAMiSSF50939. SSF50939. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNANH_CLOSO
AccessioniPrimary (citable) accession number: P15698
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: September 7, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.