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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

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. 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.
PIRi E82158.
RefSeqi NP_231419.1. NC_002505.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 44 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