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Protein

Sialidase

Gene

nanH

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves the terminal sialic acid (N-acetyl neuraminic acid) from carbohydrate chains in glycoproteins providing free sialic acid which can be used as carbon and energy sources. Sialidases have been suggested to be pathogenic factors in microbial infections. Facilitates cholera toxin binding to host intestinal epithelial cells by converting cell surface polysialogangliosides to GM1 monogangliosides.

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.

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei224SubstrateBy similarity1
Active sitei250Proton acceptorBy similarity1
Active sitei619Sequence analysis1
Binding sitei635SubstrateBy similarity1
Binding sitei712SubstrateBy similarity1
Active sitei740NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BRENDAi3.2.1.18. 6626.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Sialidase (EC:3.2.1.18)
Alternative name(s):
Neuraminidase
Short name:
NANase
Gene namesi
Name:nanH
Ordered Locus Names:VC_1784
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000000584 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075100.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24By similarityAdd BLAST24
ChainiPRO_000001203325 – 781SialidaseAdd BLAST757

Expressioni

Inductioni

May be controlled by sialic acid availability and a growth-phase-dependent mechanism.

Interactioni

Subunit structurei

Monomer.Curated

Protein-protein interaction databases

STRINGi243277.VC1784.

Chemistry databases

BindingDBiP0C6E9.

Structurei

Secondary structure

1781
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi26 – 30Combined sources5
Helixi35 – 37Combined sources3
Helixi40 – 43Combined sources4
Beta strandi54 – 62Combined sources9
Beta strandi64 – 73Combined sources10
Beta strandi75 – 79Combined sources5
Helixi83 – 92Combined sources10
Beta strandi94 – 106Combined sources13
Beta strandi111 – 113Combined sources3
Beta strandi115 – 119Combined sources5
Beta strandi121 – 125Combined sources5
Beta strandi131 – 135Combined sources5
Beta strandi142 – 145Combined sources4
Helixi147 – 151Combined sources5
Beta strandi154 – 161Combined sources8
Beta strandi163 – 165Combined sources3
Beta strandi167 – 172Combined sources6
Beta strandi175 – 181Combined sources7
Beta strandi190 – 195Combined sources6
Beta strandi198 – 200Combined sources3
Beta strandi202 – 213Combined sources12
Beta strandi216 – 219Combined sources4
Beta strandi224 – 230Combined sources7
Beta strandi232 – 234Combined sources3
Beta strandi238 – 246Combined sources9
Beta strandi257 – 271Combined sources15
Beta strandi276 – 279Combined sources4
Helixi280 – 282Combined sources3
Beta strandi284 – 286Combined sources3
Beta strandi288 – 298Combined sources11
Turni299 – 302Combined sources4
Beta strandi303 – 312Combined sources10
Helixi318 – 320Combined sources3
Beta strandi329 – 336Combined sources8
Turni337 – 340Combined sources4
Beta strandi341 – 347Combined sources7
Helixi349 – 352Combined sources4
Beta strandi357 – 371Combined sources15
Beta strandi380 – 392Combined sources13
Beta strandi394 – 411Combined sources18
Beta strandi417 – 421Combined sources5
Beta strandi428 – 431Combined sources4
Helixi434 – 437Combined sources4
Beta strandi441 – 448Combined sources8
Turni449 – 452Combined sources4
Beta strandi453 – 458Combined sources6
Beta strandi461 – 466Combined sources6
Beta strandi474 – 480Combined sources7
Beta strandi483 – 485Combined sources3
Beta strandi487 – 498Combined sources12
Beta strandi501 – 506Combined sources6
Helixi508 – 512Combined sources5
Helixi522 – 524Combined sources3
Beta strandi528 – 534Combined sources7
Beta strandi536 – 540Combined sources5
Beta strandi542 – 545Combined sources4
Beta strandi568 – 578Combined sources11
Beta strandi580 – 593Combined sources14
Beta strandi595 – 599Combined sources5
Beta strandi604 – 610Combined sources7
Beta strandi612 – 614Combined sources3
Beta strandi616 – 624Combined sources9
Beta strandi630 – 638Combined sources9
Beta strandi649 – 661Combined sources13
Beta strandi663 – 669Combined sources7
Helixi670 – 672Combined sources3
Beta strandi684 – 689Combined sources6
Beta strandi695 – 702Combined sources8
Turni704 – 708Combined sources5
Beta strandi709 – 722Combined sources14
Beta strandi728 – 732Combined sources5
Beta strandi735 – 737Combined sources3
Beta strandi740 – 745Combined sources6
Beta strandi747 – 756Combined sources10
Helixi758 – 760Combined sources3
Beta strandi762 – 768Combined sources7
Helixi769 – 772Combined sources4
Helixi773 – 775Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KITX-ray2.30A25-781[»]
1W0OX-ray1.90A1-781[»]
1W0PX-ray1.60A1-781[»]
2W68X-ray2.50A/B/C25-216[»]
ProteinModelPortaliP0C6E9.
SMRiP0C6E9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C6E9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati263 – 274BNR 1Add BLAST12
Repeati585 – 596BNR 2Add BLAST12
Repeati653 – 664BNR 3Add BLAST12
Repeati718 – 729BNR 4Add BLAST12

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4108478. Bacteria.
COG4409. LUCA.
KOiK01186.

Family and domain databases

Gene3Di2.120.10.10. 2 hits.
2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
IPR015344. VCNA_lectin-like_dom.
[Graphical view]
PANTHERiPTHR10628. PTHR10628. 2 hits.
PfamiPF13088. BNR_2. 1 hit.
PF09264. Sial-lect-inser. 2 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.
SSF50939. SSF50939. 2 hits.

Sequencei

Sequence statusi: Complete.

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

P0C6E9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFKNVKKTA LMLAMFGMAT SSNAALFDYN ATGDTEFDSP AKQGWMQDNT
60 70 80 90 100
NNGSGVLTNA DGMPAWLVQG IGGRAQWTYS LSTNQHAQAS SFGWRMTTEM
110 120 130 140 150
KVLSGGMITN YYANGTQRVL PIISLDSSGN LVVEFEGQTG RTVLATGTAA
160 170 180 190 200
TEYHKFELVF LPGSNPSASF YFDGKLIRDN IQPTASKQNM IVWGNGSSNT
210 220 230 240 250
DGVAAYRDIK FEIQGDVIFR GPDRIPSIVA SSVTPGVVTA FAEKRVGGGD
260 270 280 290 300
PGALSNTNDI ITRTSRDGGI TWDTELNLTE QINVSDEFDF SDPRPIYDPS
310 320 330 340 350
SNTVLVSYAR WPTDAAQNGD RIKPWMPNGI FYSVYDVASG NWQAPIDVTD
360 370 380 390 400
QVKERSFQIA GWGGSELYRR NTSLNSQQDW QSNAKIRIVD GAANQIQVAD
410 420 430 440 450
GSRKYVVTLS IDESGGLVAN LNGVSAPIIL QSEHAKVHSF HDYELQYSAL
460 470 480 490 500
NHTTTLFVDG QQITTWAGEV SQENNIQFGN ADAQIDGRLH VQKIVLTQQG
510 520 530 540 550
HNLVEFDAFY LAQQTPEVEK DLEKLGWTKI KTGNTMSLYG NASVNPGPGH
560 570 580 590 600
GITLTRQQNI SGSQNGRLIY PAIVLDRFFL NVMSIYSDDG GSNWQTGSTL
610 620 630 640 650
PIPFRWKSSS ILETLEPSEA DMVELQNGDL LLTARLDFNQ IVNGVNYSPR
660 670 680 690 700
QQFLSKDGGI TWSLLEANNA NVFSNISTGT VDASITRFEQ SDGSHFLLFT
710 720 730 740 750
NPQGNPAGTN GRQNLGLWFS FDEGVTWKGP IQLVNGASAY SDIYQLDSEN
760 770 780
AIVIVETDNS NMRILRMPIT LLKQKLTLSQ N
Length:781
Mass (Da):85,609
Last modified:March 18, 2008 - v1
Checksum:iFA85ED907FB20AF0
GO

Sequence cautioni

The sequence AAF94933 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF94933.1. Different initiation.
PIRiE82158.
RefSeqiNP_231419.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF94933; AAF94933; VC_1784.
GeneIDi2613664.
KEGGivch:VC1784.
PATRICi20082616. VBIVibCho83274_1703.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF94933.1. Different initiation.
PIRiE82158.
RefSeqiNP_231419.1. NC_002505.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KITX-ray2.30A25-781[»]
1W0OX-ray1.90A1-781[»]
1W0PX-ray1.60A1-781[»]
2W68X-ray2.50A/B/C25-216[»]
ProteinModelPortaliP0C6E9.
SMRiP0C6E9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243277.VC1784.

Chemistry databases

BindingDBiP0C6E9.
ChEMBLiCHEMBL1075100.

Protein family/group databases

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

Protocols and materials databases

DNASUi2613664.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF94933; AAF94933; VC_1784.
GeneIDi2613664.
KEGGivch:VC1784.
PATRICi20082616. VBIVibCho83274_1703.

Phylogenomic databases

eggNOGiENOG4108478. Bacteria.
COG4409. LUCA.
KOiK01186.

Enzyme and pathway databases

BRENDAi3.2.1.18. 6626.

Miscellaneous databases

EvolutionaryTraceiP0C6E9.
PROiP0C6E9.

Family and domain databases

Gene3Di2.120.10.10. 2 hits.
2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
IPR015344. VCNA_lectin-like_dom.
[Graphical view]
PANTHERiPTHR10628. PTHR10628. 2 hits.
PfamiPF13088. BNR_2. 1 hit.
PF09264. Sial-lect-inser. 2 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.
SSF50939. SSF50939. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiNANH_VIBCH
AccessioniPrimary (citable) accession number: P0C6E9
Secondary accession number(s): P37060, Q9KR59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: November 2, 2016
This is version 59 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

3D-structure, Complete proteome, Reference proteome

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.