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Protein

Anhydrosialidase

Gene
N/A
Organism
Macrobdella decora (North American leech)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei293Substrate1
Active sitei318Proton acceptor1
Active sitei5951
Binding sitei611Substrate1
Binding sitei673Substrate1
Active sitei713Nucleophile1

GO - Molecular functioni

GO - Biological processi

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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
ChainiPRO_000001204028 – 762AnhydrosialidaseAdd BLAST735

Proteomic databases

PRIDEiQ27701.

Structurei

Secondary structure

1762
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi83 – 94Combined sources12
Turni96 – 98Combined sources3
Helixi108 – 111Combined sources4
Beta strandi115 – 125Combined sources11
Beta strandi130 – 138Combined sources9
Beta strandi147 – 154Combined sources8
Beta strandi159 – 165Combined sources7
Turni167 – 169Combined sources3
Beta strandi171 – 178Combined sources8
Beta strandi182 – 184Combined sources3
Beta strandi191 – 198Combined sources8
Turni199 – 202Combined sources4
Beta strandi203 – 208Combined sources6
Beta strandi211 – 217Combined sources7
Helixi224 – 226Combined sources3
Beta strandi232 – 240Combined sources9
Beta strandi243 – 246Combined sources4
Beta strandi250 – 260Combined sources11
Helixi264 – 271Combined sources8
Beta strandi290 – 299Combined sources10
Beta strandi305 – 314Combined sources10
Beta strandi319 – 321Combined sources3
Beta strandi323 – 332Combined sources10
Beta strandi341 – 344Combined sources4
Helixi362 – 364Combined sources3
Beta strandi372 – 381Combined sources10
Turni382 – 385Combined sources4
Beta strandi386 – 394Combined sources9
Helixi400 – 402Combined sources3
Beta strandi408 – 412Combined sources5
Beta strandi415 – 422Combined sources8
Beta strandi432 – 434Combined sources3
Helixi436 – 438Combined sources3
Beta strandi439 – 442Combined sources4
Turni443 – 446Combined sources4
Beta strandi447 – 453Combined sources7
Beta strandi458 – 461Combined sources4
Beta strandi467 – 476Combined sources10
Beta strandi479 – 490Combined sources12
Beta strandi499 – 502Combined sources4
Beta strandi507 – 515Combined sources9
Helixi527 – 529Combined sources3
Beta strandi535 – 539Combined sources5
Beta strandi541 – 543Combined sources3
Turni551 – 554Combined sources4
Beta strandi556 – 565Combined sources10
Beta strandi567 – 575Combined sources9
Beta strandi581 – 584Combined sources4
Beta strandi596 – 600Combined sources5
Beta strandi606 – 610Combined sources5
Beta strandi613 – 616Combined sources4
Beta strandi618 – 624Combined sources7
Beta strandi648 – 656Combined sources9
Beta strandi659 – 667Combined sources9
Beta strandi670 – 674Combined sources5
Beta strandi676 – 685Combined sources10
Helixi690 – 692Combined sources3
Beta strandi693 – 705Combined sources13
Beta strandi714 – 718Combined sources5
Beta strandi720 – 722Combined sources3
Beta strandi724 – 729Combined sources6
Beta strandi745 – 750Combined sources6
Helixi752 – 755Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ27701.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati328 – 339BNR 1Add BLAST12
Repeati511 – 522BNR 2Add BLAST12
Repeati571 – 582BNR 3Add BLAST12
Repeati620 – 631BNR 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. 2 hits.
2.40.220.10. 1 hit.
2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR004124. Glyco_hydro_33_N.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
IPR023364. Trans_sialidase_dom3.
[Graphical view]
PANTHERiPTHR10628. PTHR10628. 2 hits.
PfamiPF13088. BNR_2. 1 hit.
PF02973. Sialidase. 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:
EMBLi
GenBanki
DDBJi
Links Updated
U46666 mRNA. Translation: AAC47263.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U46666 mRNA. Translation: AAC47263.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

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

Proteomic databases

PRIDEiQ27701.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ27701.

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.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
IPR023364. Trans_sialidase_dom3.
[Graphical view]
PANTHERiPTHR10628. PTHR10628. 2 hits.
PfamiPF13088. BNR_2. 1 hit.
PF02973. Sialidase. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF50939. SSF50939. 2 hits.
ProtoNetiSearch...

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: November 2, 2016
This is version 96 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

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.