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P0C6E9

- NANH_VIBCH

UniProt

P0C6E9 - NANH_VIBCH

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Protein

Sialidase

Gene

nanH

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed - Annotation score: 4 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

Calcium.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei224 – 2241SubstrateBy similarity
Active sitei250 – 2501Proton acceptorBy similarity
Active sitei619 – 6191Sequence Analysis
Binding sitei635 – 6351SubstrateBy similarity
Binding sitei712 – 7121SubstrateBy similarity
Active sitei740 – 7401NucleophileBy similarity

GO - Molecular functioni

  1. exo-alpha-(2->3)-sialidase activity Source: UniProtKB-EC
  2. exo-alpha-(2->6)-sialidase activity Source: UniProtKB-EC
  3. exo-alpha-(2->8)-sialidase activity Source: UniProtKB-EC
  4. sialic acid binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium

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
ProteomesiUP000000584: Chromosome 1

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 – 2424By similarityAdd
BLAST
Chaini25 – 781757SialidasePRO_0000012033Add
BLAST

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.

Structurei

Secondary structure

1
781
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 305
Helixi35 – 373
Helixi40 – 434
Beta strandi54 – 629
Beta strandi64 – 7310
Beta strandi75 – 795
Helixi83 – 9210
Beta strandi94 – 10613
Beta strandi111 – 1133
Beta strandi115 – 1195
Beta strandi121 – 1255
Beta strandi131 – 1355
Beta strandi142 – 1454
Helixi147 – 1515
Beta strandi154 – 1618
Beta strandi163 – 1653
Beta strandi167 – 1726
Beta strandi175 – 1817
Beta strandi190 – 1956
Beta strandi198 – 2003
Beta strandi202 – 21312
Beta strandi216 – 2194
Beta strandi224 – 2307
Beta strandi232 – 2343
Beta strandi238 – 2469
Beta strandi257 – 27115
Beta strandi276 – 2794
Helixi280 – 2823
Beta strandi284 – 2863
Beta strandi288 – 29811
Turni299 – 3024
Beta strandi303 – 31210
Helixi318 – 3203
Beta strandi329 – 3368
Turni337 – 3404
Beta strandi341 – 3477
Helixi349 – 3524
Beta strandi357 – 37115
Beta strandi380 – 39213
Beta strandi394 – 41118
Beta strandi417 – 4215
Beta strandi428 – 4314
Helixi434 – 4374
Beta strandi441 – 4488
Turni449 – 4524
Beta strandi453 – 4586
Beta strandi461 – 4666
Beta strandi474 – 4807
Beta strandi483 – 4853
Beta strandi487 – 49812
Beta strandi501 – 5066
Helixi508 – 5125
Helixi522 – 5243
Beta strandi528 – 5347
Beta strandi536 – 5405
Beta strandi542 – 5454
Beta strandi568 – 57811
Beta strandi580 – 59314
Beta strandi595 – 5995
Beta strandi604 – 6107
Beta strandi612 – 6143
Beta strandi616 – 6249
Beta strandi630 – 6389
Beta strandi649 – 66113
Beta strandi663 – 6697
Helixi670 – 6723
Beta strandi684 – 6896
Beta strandi695 – 7028
Turni704 – 7085
Beta strandi709 – 72214
Beta strandi728 – 7325
Beta strandi735 – 7373
Beta strandi740 – 7456
Beta strandi747 – 75610
Helixi758 – 7603
Beta strandi762 – 7687
Helixi769 – 7724
Helixi773 – 7753

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KITX-ray2.30A25-781[»]
1W0OX-ray1.90A1-781[»]
1W0PX-ray1.60A1-781[»]
2W68X-ray2.50A/B/C25-216[»]
ProteinModelPortaliP0C6E9.
SMRiP0C6E9. Positions 25-781.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C6E9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati263 – 27412BNR 1Add
BLAST
Repeati585 – 59612BNR 2Add
BLAST
Repeati653 – 66412BNR 3Add
BLAST
Repeati718 – 72912BNR 4Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG4409.
KOiK01186.
OrthoDBiEOG64JFJ7.

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. 1 hit.
PfamiPF09264. 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 AAF94933.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE003852 Genomic DNA. Translation: AAF94933.1 . Different initiation.
PIRi E82158.
RefSeqi NP_231419.1. NC_002505.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KIT X-ray 2.30 A 25-781 [» ]
1W0O X-ray 1.90 A 1-781 [» ]
1W0P X-ray 1.60 A 1-781 [» ]
2W68 X-ray 2.50 A/B/C 25-216 [» ]
ProteinModelPortali P0C6E9.
SMRi P0C6E9. Positions 25-781.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243277.VC1784.

Chemistry

BindingDBi P0C6E9.
ChEMBLi CHEMBL1075100.

Protocols and materials databases

DNASUi 2613664.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF94933 ; AAF94933 ; VC_1784 .
GeneIDi 2613664.
KEGGi vch:VC1784.
PATRICi 20082616. VBIVibCho83274_1703.

Phylogenomic databases

eggNOGi COG4409.
KOi K01186.
OrthoDBi EOG64JFJ7.

Miscellaneous databases

EvolutionaryTracei P0C6E9.

Family and domain databases

Gene3Di 2.120.10.10. 2 hits.
2.60.120.200. 2 hits.
InterProi IPR013320. ConA-like_dom.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
IPR015344. VCNA_lectin-like_dom.
[Graphical view ]
PANTHERi PTHR10628. PTHR10628. 1 hit.
Pfami PF09264. Sial-lect-inser. 2 hits.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 2 hits.
SSF50939. SSF50939. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39315 / El Tor Inaba N16961.
  2. "Purification, crystallization and preliminary crystallographic study of neuraminidase from Vibrio cholerae and Salmonella typhimurium LT2."
    Taylor G.L., Vimr E.R., Garman E.F., Laver W.G.
    J. Mol. Biol. 226:1287-1290(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  3. "Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain."
    Crenells S., Garman E.F., Laver W.G., Vimr E.R., Taylor G.L.
    Structure 2:535-544(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

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: October 29, 2014
This is version 43 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

External Data

Dasty 3