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Q27701

- NANL_MACDE

UniProt

Q27701 - NANL_MACDE

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Protein

Anhydrosialidase

Gene
N/A
Organism
Macrobdella decora (North American leech)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei293 – 2931Substrate
Active sitei318 – 3181Proton acceptor
Active sitei595 – 5951
Binding sitei611 – 6111Substrate
Binding sitei673 – 6731Substrate
Active sitei713 – 7131Nucleophile

GO - Molecular functioni

  1. anhydrosialidase activity Source: UniProtKB-EC
  2. exo-alpha-sialidase activity Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Lyase

Protein family/group databases

CAZyiCBM40. Carbohydrate-Binding Module Family 40.
GH33. Glycoside Hydrolase Family 33.

Names & Taxonomyi

Protein namesi
Recommended name:
Anhydrosialidase (EC:4.2.2.15)
Alternative name(s):
Anhydroneuraminidase
Sialidase L
OrganismiMacrobdella decora (North American leech)
Taxonomic identifieri6405 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaAnnelidaClitellataHirudinidaHirudineaArhynchobdellidaHirudiniformesHirudinidaeMacrobdella

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 762735AnhydrosialidasePRO_0000012040Add
BLAST

Structurei

Secondary structure

1
762
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi83 – 9412
Turni96 – 983
Helixi108 – 1114
Beta strandi115 – 12511
Beta strandi130 – 1389
Beta strandi147 – 1548
Beta strandi159 – 1657
Turni167 – 1693
Beta strandi171 – 1788
Beta strandi182 – 1843
Beta strandi191 – 1988
Turni199 – 2024
Beta strandi203 – 2086
Beta strandi211 – 2177
Helixi224 – 2263
Beta strandi232 – 2409
Beta strandi243 – 2464
Beta strandi250 – 26011
Helixi264 – 2718
Beta strandi290 – 29910
Beta strandi305 – 31410
Beta strandi319 – 3213
Beta strandi323 – 33210
Beta strandi341 – 3444
Helixi362 – 3643
Beta strandi372 – 38110
Turni382 – 3854
Beta strandi386 – 3949
Helixi400 – 4023
Beta strandi408 – 4125
Beta strandi415 – 4228
Beta strandi432 – 4343
Helixi436 – 4383
Beta strandi439 – 4424
Turni443 – 4464
Beta strandi447 – 4537
Beta strandi458 – 4614
Beta strandi467 – 47610
Beta strandi479 – 49012
Beta strandi499 – 5024
Beta strandi507 – 5159
Helixi527 – 5293
Beta strandi535 – 5395
Beta strandi541 – 5433
Turni551 – 5544
Beta strandi556 – 56510
Beta strandi567 – 5759
Beta strandi581 – 5844
Beta strandi596 – 6005
Beta strandi606 – 6105
Beta strandi613 – 6164
Beta strandi618 – 6247
Beta strandi648 – 6569
Beta strandi659 – 6679
Beta strandi670 – 6745
Beta strandi676 – 68510
Helixi690 – 6923
Beta strandi693 – 70513
Beta strandi714 – 7185
Beta strandi720 – 7223
Beta strandi724 – 7296
Beta strandi745 – 7506
Helixi752 – 7554

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SLIX-ray2.00A81-759[»]
1SLLX-ray2.00A81-759[»]
2SLIX-ray1.80A81-759[»]
3SLIX-ray1.80A81-759[»]
4SLIX-ray1.80A81-759[»]
ProteinModelPortaliQ27701.
SMRiQ27701. Positions 81-759.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ27701.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati328 – 33912BNR 1Add
BLAST
Repeati511 – 52212BNR 2Add
BLAST
Repeati571 – 58212BNR 3Add
BLAST
Repeati620 – 63112BNR 4Add
BLAST

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. 2 hits.
2.40.220.10. 1 hit.
2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR004124. Glyco_hydro_33_N.
IPR001791. Laminin_G.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
IPR023364. Trans_sialidase_dom3.
[Graphical view]
PANTHERiPTHR10628. PTHR10628. 1 hit.
PfamiPF02973. Sialidase. 1 hit.
[Graphical view]
SMARTiSM00282. LamG. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF50939. SSF50939. 2 hits.

Sequencei

Sequence statusi: Complete.

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

Q27701-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGRIGKKAMA IALVSAVMVT PLNVCATVEN QEQQQVTQGA EDIAVIDDAQ
60 70 80 90 100
ETVAADEAQA DEAAAITVEG RETAEESSAS IPEGILMEKN NVDIAEGQGY
110 120 130 140 150
SLDQEAGAKY VKAMTQGTII LSYKSTSENG IQSLFSVGNS TAGNQDRHFH
160 170 180 190 200
IYITNSGGIG IELRNTDGVF NYTLDRPASV RALYKGERVF NTVALKADAA
210 220 230 240 250
NKQCRLFANG ELLATLDKDA FKFISDITGV DNVTLGGTKR QGKIAYPFGG
260 270 280 290 300
TIGDIKVYSN ALSDEELIQA TGVTTYGENI FYAGDVTESN YFRIPSLLTL
310 320 330 340 350
STGTVISAAD ARYGGTHDSK SKINIAFAKS TDGGNTWSEP TLPLKFDDYI
360 370 380 390 400
AKNIDWPRDS VGKNVQIQGS ASYIDPVLLE DKLTKRIFLF ADLMPAGIGS
410 420 430 440 450
SNASVGSGFK EVNGKKYLKL RWHKDAGRAY DYTIREKGVI YNDATNQPTE
460 470 480 490 500
FRVDGEYNLY QHDTNLTCKQ YDYNFSGNNL IESKTDVDVN MNIFYKNSVF
510 520 530 540 550
KAFPTNYLAM RYSDDEGASW SDLDIVSSFK PEVSKFLVVG PGIGKQISTG
560 570 580 590 600
ENAGRLLVPL YSKSSAELGF MYSDDHGDNW TYVEADNLTG GATAEAQIVE
610 620 630 640 650
MPDGSLKTYL RTGSNCIAEV TSIDGGETWS DRVPLQGIST TSYGTQLSVI
660 670 680 690 700
NYSQPIDGKP AIILSSPNAT NGRKNGKIWI GLVNDTGNTG IDKYSVEWKY
710 720 730 740 750
SYAVDTPQMG YSYSCLAELP DGQVGLLYEK YDSWSRNELH LKDILKFEKY
760
SISELTGQAS GN
Length:762
Mass (Da):82,982
Last modified:November 1, 1996 - v1
Checksum:iC0C547C7A8632B37
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U46666 mRNA. Translation: AAC47263.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U46666 mRNA. Translation: AAC47263.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SLI X-ray 2.00 A 81-759 [» ]
1SLL X-ray 2.00 A 81-759 [» ]
2SLI X-ray 1.80 A 81-759 [» ]
3SLI X-ray 1.80 A 81-759 [» ]
4SLI X-ray 1.80 A 81-759 [» ]
ProteinModelPortali Q27701.
SMRi Q27701. Positions 81-759.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM40. Carbohydrate-Binding Module Family 40.
GH33. Glycoside Hydrolase Family 33.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q27701.

Family and domain databases

Gene3Di 2.120.10.10. 2 hits.
2.40.220.10. 1 hit.
2.60.120.200. 1 hit.
InterProi IPR013320. ConA-like_dom.
IPR004124. Glyco_hydro_33_N.
IPR001791. Laminin_G.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
IPR023364. Trans_sialidase_dom3.
[Graphical view ]
PANTHERi PTHR10628. PTHR10628. 1 hit.
Pfami PF02973. Sialidase. 1 hit.
[Graphical view ]
SMARTi SM00282. LamG. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF50939. SSF50939. 2 hits.
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 81-759.

Entry informationi

Entry nameiNANL_MACDE
AccessioniPrimary (citable) accession number: Q27701
Secondary accession number(s): Q9TWN0, Q9TWN1, Q9TWN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3