A5F7A4 (NANH_VIBC3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sialidase
EC=3.2.1.18

Alternative name(s):
Neuraminidase
Short name=NANase

Gene names

Name:	nanH
Ordered Locus Names:	VC0395_A1381, VC395_1898

Organism

Vibrio cholerae serotype O1 (strain ATCC 39541 / Ogawa 395 / O395) [Complete proteome] [HAMAP]

Taxonomic identifier

345073 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › Vibrio cholerae

Protein attributes

Sequence length	781 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	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.
Cofactor	Calcium By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Secreted.
Induction	May be controlled by sialic acid availability and a growth-phase-dependent mechanism.
Sequence similarities	Belongs to the glycosyl hydrolase 33 family. Contains 4 BNR repeats.
Sequence caution	The sequence ABQ19703.1 differs from that shown. Reason: Erroneous initiation. The sequence ACP09894.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Calcium
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	exo-alpha-(2->3)-sialidase activity Inferred from electronic annotation. Source: EC exo-alpha-(2->6)-sialidase activity Inferred from electronic annotation. Source: EC exo-alpha-(2->8)-sialidase activity Inferred from electronic annotation. Source: EC sialic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Ref.4
	Chain	25 – 781	757	Sialidase		PRO_0000323013
Regions
	Repeat	263 – 274	12	BNR 1
	Repeat	585 – 596	12	BNR 2
	Repeat	653 – 664	12	BNR 3
	Repeat	718 – 729	12	BNR 4
Sites
	Active site	250	1	Proton acceptor By similarity
	Active site	619	1	Potential
	Active site	740	1	Nucleophile By similarity
	Binding site	224	1	Substrate By similarity
	Binding site	635	1	Substrate By similarity
	Binding site	712	1	Substrate By similarity
Experimental info
	Sequence conflict	22	1	S → L in AAA27547. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	A5F7A4 [UniParc]. Last modified March 18, 2008. Version 2. Checksum: FA85ED907FB20AF0	FASTA	781	85,609
	10 20 30 40 50 60 MRFKNVKKTA LMLAMFGMAT SSNAALFDYN ATGDTEFDSP AKQGWMQDNT NNGSGVLTNA 70 80 90 100 110 120 DGMPAWLVQG IGGRAQWTYS LSTNQHAQAS SFGWRMTTEM KVLSGGMITN YYANGTQRVL 130 140 150 160 170 180 PIISLDSSGN LVVEFEGQTG RTVLATGTAA TEYHKFELVF LPGSNPSASF YFDGKLIRDN 190 200 210 220 230 240 IQPTASKQNM IVWGNGSSNT DGVAAYRDIK FEIQGDVIFR GPDRIPSIVA SSVTPGVVTA 250 260 270 280 290 300 FAEKRVGGGD PGALSNTNDI ITRTSRDGGI TWDTELNLTE QINVSDEFDF SDPRPIYDPS 310 320 330 340 350 360 SNTVLVSYAR WPTDAAQNGD RIKPWMPNGI FYSVYDVASG NWQAPIDVTD QVKERSFQIA 370 380 390 400 410 420 GWGGSELYRR NTSLNSQQDW QSNAKIRIVD GAANQIQVAD GSRKYVVTLS IDESGGLVAN 430 440 450 460 470 480 LNGVSAPIIL QSEHAKVHSF HDYELQYSAL NHTTTLFVDG QQITTWAGEV SQENNIQFGN 490 500 510 520 530 540 ADAQIDGRLH VQKIVLTQQG HNLVEFDAFY LAQQTPEVEK DLEKLGWTKI KTGNTMSLYG 550 560 570 580 590 600 NASVNPGPGH GITLTRQQNI SGSQNGRLIY PAIVLDRFFL NVMSIYSDDG GSNWQTGSTL 610 620 630 640 650 660 PIPFRWKSSS ILETLEPSEA DMVELQNGDL LLTARLDFNQ IVNGVNYSPR QQFLSKDGGI 670 680 690 700 710 720 TWSLLEANNA NVFSNISTGT VDASITRFEQ SDGSHFLLFT NPQGNPAGTN GRQNLGLWFS 730 740 750 760 770 780 FDEGVTWKGP IQLVNGASAY SDIYQLDSEN AIVIVETDNS NMRILRMPIT LLKQKLTLSQ N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Role of Vibrio cholerae neuraminidase in the function of cholera toxin." Galen J.E., Ketley J.M., Fasano A., Richardson S.H., Wasserman S.S., Kaper J.B. Infect. Immun. 60:406-415(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Heidelberg J. Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39541 / Ogawa 395 / O395.
[3]	"A recalibrated molecular clock and independent origins for the cholera pandemic clones." Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L. PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39541 / Ogawa 395 / O395.
[4]	"Cloning and expression of the Vibrio cholerae neuraminidase gene nanH in Escherichia coli." Vimr E.R., Lawrisuk L., Galen J.E., Kaper J.B. J. Bacteriol. 170:1495-1504(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44, PROTEIN SEQUENCE OF 25-44.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M83562 Genomic DNA. Translation: AAA27546.1. CP000627 Genomic DNA. Translation: ABQ19703.1. Different initiation. CP001235 Genomic DNA. Translation: ACP09894.1. Different initiation. M19268 Genomic DNA. Translation: AAA27547.1.
PIR	A27734. A43866.
RefSeq	YP_001217324.1. NC_009457.1. YP_002820130.1. NC_012582.1.
3D structure databases
ProteinModelPortal	A5F7A4.
SMR	A5F7A4. Positions 25-781.
ModBase	Search...
Protein-protein interaction databases
STRING	345073.VC0395_A1381.
Protein family/group databases
CAZy	CBM40. Carbohydrate-Binding Module Family 40. GH33. Glycoside Hydrolase Family 33.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABQ19703; ABQ19703; VC0395_A1381. ACP09894; ACP09894; VC395_1898.
GeneID	5137230. 7775747.
KEGG	vco:VC0395_A1381. vcr:VC395_1898.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG4409.
HOGENOM	HOG000218204.
KO	K01186.
ProtClustDB	CLSK794375.
Family and domain databases
Gene3D	2.120.10.10. 2 hits. 2.60.120.200. 2 hits.
InterPro	IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. IPR026856. Sialidase_fam. IPR011040. Sialidases. IPR015344. VCNA_lectin-like_dom. [Graphical view]
PANTHER	PTHR10628. PTHR10628. 1 hit.
Pfam	PF09264. Sial-lect-inser. 2 hits. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 2 hits. SSF50939. Sialidase. 1 hit.
ProtoNet	Search...
Other
BindingDB	A5F7A4.

Entry information

Entry name

NANH_VIBC3

Accession

Primary (citable) accession number: A5F7A4
Secondary accession number(s): C3M1H8, P37060, Q9KR59

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	March 18, 2008
Last modified:	May 1, 2013
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program