Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot Q27701 (NANL_MACDE)

Last modified June 16, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Anhydrosialidase
    EC=4.2.2.15
Alternative name(s):
    Sialidase L
    Anhydroneuraminidase
OrganismMacrobdella decora (North American leech)
Taxonomic identifier6405 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Annelida › Clitellata › Hirudinida › Hirudinea › Arhynchobdellida › Hirudiniformes › Hirudinidae › Macrobdella

Hide | Top

Protein attributes

Sequence length762 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity

Elimination of alpha-sialyl groups in N-acetylneuraminic acid glycosides, releasing 2,7-anhydro-alpha-N-acetylneuraminate.

Subcellular location

Secreted › extracellular space.

Sequence similarities

Belongs to the glycosyl hydrolase 33 family.

Contains 4 BNR repeats.

Hide | Top

Ontologies

Keywords
   Cellular componentSecreted
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
Lyase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionanhydrosialidase activity

Inferred from electronic annotation. Source: EC

exo-alpha-sialidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 762735Anhydrosialidase
PRO_0000012040

Regions

Repeat328 – 33912BNR 1
Repeat511 – 52212BNR 2
Repeat571 – 58212BNR 3
Repeat620 – 63112BNR 4

Sites

Active site3181Proton acceptor
Active site5951
Active site7131Nucleophile
Binding site2931Substrate
Binding site6111Substrate
Binding site6731Substrate

Secondary structure

1 ......................................................................................................................... 762
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q27701-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C0C547C7A8632B37

FASTA76282,982
        10         20         30         40         50         60 
MGRIGKKAMA IALVSAVMVT PLNVCATVEN QEQQQVTQGA EDIAVIDDAQ ETVAADEAQA 

        70         80         90        100        110        120 
DEAAAITVEG RETAEESSAS IPEGILMEKN NVDIAEGQGY SLDQEAGAKY VKAMTQGTII 

       130        140        150        160        170        180 
LSYKSTSENG IQSLFSVGNS TAGNQDRHFH IYITNSGGIG IELRNTDGVF NYTLDRPASV 

       190        200        210        220        230        240 
RALYKGERVF NTVALKADAA NKQCRLFANG ELLATLDKDA FKFISDITGV DNVTLGGTKR 

       250        260        270        280        290        300 
QGKIAYPFGG TIGDIKVYSN ALSDEELIQA TGVTTYGENI FYAGDVTESN YFRIPSLLTL 

       310        320        330        340        350        360 
STGTVISAAD ARYGGTHDSK SKINIAFAKS TDGGNTWSEP TLPLKFDDYI AKNIDWPRDS 

       370        380        390        400        410        420 
VGKNVQIQGS ASYIDPVLLE DKLTKRIFLF ADLMPAGIGS SNASVGSGFK EVNGKKYLKL 

       430        440        450        460        470        480 
RWHKDAGRAY DYTIREKGVI YNDATNQPTE FRVDGEYNLY QHDTNLTCKQ YDYNFSGNNL 

       490        500        510        520        530        540 
IESKTDVDVN MNIFYKNSVF KAFPTNYLAM RYSDDEGASW SDLDIVSSFK PEVSKFLVVG 

       550        560        570        580        590        600 
PGIGKQISTG ENAGRLLVPL YSKSSAELGF MYSDDHGDNW TYVEADNLTG GATAEAQIVE 

       610        620        630        640        650        660 
MPDGSLKTYL RTGSNCIAEV TSIDGGETWS DRVPLQGIST TSYGTQLSVI NYSQPIDGKP 

       670        680        690        700        710        720 
AIILSSPNAT NGRKNGKIWI GLVNDTGNTG IDKYSVEWKY SYAVDTPQMG YSYSCLAELP 

       730        740        750        760 
DGQVGLLYEK YDSWSRNELH LKDILKFEKY SISELTGQAS GN

« Hide

Hide | Top

References

[1]"Cloning and expression of sialidase L, a NeuAc-alpha2-->3Gal-specific sialidase from the leech, Macrobdella decora."
Chou M.-Y., Li S.-C., Li Y.-T.
J. Biol. Chem. 271:19219-19224(1996) [PubMed: 8702601] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Purification and characterization of sialidase L, a NeuAc-alpha 2-->3Gal-specific sialidase."
Chou M.-Y., Li S.-C., Kiso M., Hasegawa A., Li Y.-T.
J. Biol. Chem. 269:18821-18826(1994) [PubMed: 8034634] [Abstract]
Cited for: PROTEIN SEQUENCE OF 89-104; 330-338; 346-352; 387-406; 429-435; 438-469 AND 512-530, CHARACTERIZATION.
[3]"The crystal structure of an intramolecular trans-sialidase with a NeuAc-alpha2-->3Gal specificity."
Luo Y., Li S.-C., Chou M.-Y., Li Y.-T., Luo M.
Structure 6:521-530(1998) [PubMed: 9562562] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 81-759.
[4]"The 1.8 A structures of leech intramolecular trans-sialidase complexes: evidence of its enzymatic mechanism."
Luo Y., Li S.-C., Li Y.-T., Luo M.
J. Mol. Biol. 285:323-332(1999) [PubMed: 9878409] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 81-759.

Hide | Top

Cross-references

Sequence databases

U46666 mRNA. Translation: AAC47263.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1SLIX-ray2.00A81-759[»]
1SLLX-ray2.00A81-759[»]
2SLIX-ray1.80A81-759[»]
3SLIX-ray1.80A81-759[»]
4SLIX-ray1.80A81-759[»]
ModBaseSearch...

Protein family/group databases

CAZyCBM40. Carbohydrate-Binding Module Family 40.
GH33. Glycoside Hydrolase Family 33.

Enzyme and pathway databases

BRENDA4.2.2.15. 274178.

Family and domain databases

InterProIPR013320. ConA-like_subgrp.
IPR004124. Glyco_hydro_33_N.
IPR001791. Laminin_G.
[Graphical view]
Gene3DG3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.
PfamPF02973. Sialidase. 1 hit.
[Graphical view]
SMARTSM00282. LamG. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameNANL_MACDE
AccessionPrimary (citable) accession number: Q27701
Secondary accession number(s): Q9TWN0, Q9TWN1, Q9TWN2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Hide | Top

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents