Reviewed, UniProtKB/Swiss-Prot P29768 (NANH_SALTY)

Names and origin

Protein names

Recommended name:
    Sialidase
    EC=3.2.1.18
Alternative name(s):
    Neuraminidase
      Short name=NANase
    N-acylneuraminate glycohydrolase
    STNA

Gene names

Name:	nanH
Ordered Locus Names:	STM0928

Organism

Salmonella typhimurium [Complete proteome] [HAMAP]

Taxonomic identifier

602 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	382 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.
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.
Subunit structure	Monomer.
Sequence similarities	Belongs to the glycosyl hydrolase 33 family. Contains 4 BNR repeats.

Ontologies

Keywords
Domain	Repeat
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	exo-alpha-sialidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 382

381

Sialidase

PRO_0000208909

Regions

Repeat

71 – 82

12

BNR 1

Repeat

145 – 156

12

BNR 2

Repeat

210 – 220

11

BNR 3

Repeat

254 – 265

12

BNR 4

Sites

Active site

62

1

Proton acceptor By similarity

Active site

342

1

Nucleophile By similarity

Active site

361

1

Binding site

37

1

Substrate

Binding site

246

1

Substrate

Binding site

309

1

Substrate

Amino acid modifications

Disulfide bond

42 ↔ 103

Experimental info

Sequence conflict

329

1

D → A in AAA27168. Ref.1

Secondary structure

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382

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Helix

29 – 31

3

Beta strand

35 – 43

9

Beta strand

49 – 58

10

Beta strand

62 – 64

3

Beta strand

66 – 78

13

Beta strand

81 – 86

6

Turn

93 – 95

3

Beta strand

97 – 108

12

Beta strand

111 – 123

13

Helix

128 – 130

3

Beta strand

133 – 136

4

Beta strand

141 – 149

9

Beta strand

155 – 157

3

Helix

161 – 168

8

Beta strand

170 – 176

7

Beta strand

178 – 180

3

Beta strand

189 – 197

9

Beta strand

204 – 219

16

Beta strand

232 – 237

6

Beta strand

240 – 245

6

Beta strand

248 – 250

3

Beta strand

254 – 261

8

Turn

267 – 271

5

Beta strand

283 – 289

7

Beta strand

292 – 300

9

Beta strand

312 – 317

6

Turn

319 – 321

3

Beta strand

324 – 331

8

Beta strand

343 – 350

8

Beta strand

353 – 362

10

Beta strand

365 – 370

6

Helix

372 – 374

3

Helix

375 – 379

5

Sequences

	Sequence		Length	Mass (Da)
	P29768-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: C15515CF9C15597E	FASTA	382	42,073
	10 20 30 40 50 60 MTVEKSVVFK AEGEHFTDQK GNTIVGSGSG GTTKYFRIPA MCTTSKGTIV VFADARHNTA 70 80 90 100 110 120 SDQSFIDTAA ARSTDGGKTW NKKIAIYNDR VNSKLSRVMD PTCIVANIQG RETILVMVGK 130 140 150 160 170 180 WNNNDKTWGA YRDKAPDTDW DLVLYKSTDD GVTFSKVETN IHDIVTKNGT ISAMLGGVGS 190 200 210 220 230 240 GLQLNDGKLV FPVQMVRTKN ITTVLNTSFI YSTDGITWSL PSGYCEGFGS ENNIIEFNAS 250 260 270 280 290 300 LVNNIRNSGL RRSFETKDFG KTWTEFPPMD KKVDNRNHGV QGSTITIPSG NKLVAAHSSA 310 320 330 340 350 360 QNKNNDYTRS DISLYAHNLY SGEVKLIDDF YPKVGNASGA GYSCLSYRKN VDKETLYVVY 370 380 EANGSIEFQD LSRHLPVIKS YN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, sequencing and distribution of the Salmonella typhimurium LT2 sialidase gene, nanH, provides evidence for interspecies gene transfer." Hoyer L.L., Hamilton A.C., Steenbergen S.M., Vimr E.R. Mol. Microbiol. 6:873-884(1992) [PubMed: 1602967] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-40. Strain: LT2.
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[3]	"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: 1518058] [Abstract] Cited for: CHARACTERIZATION, X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). Strain: LT2.
[4]	"Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase." Crennell S.J., Garman E.F., Laver W.G., Vimr E.R., Taylor G.L. Proc. Natl. Acad. Sci. U.S.A. 90:9852-9856(1993) [PubMed: 8234325] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SEQUENCE REVISION TO C-TERMINUS. Strain: LT2.
[5]	"The structures of Salmonella typhimurium LT2 neuraminidase and its complexes with three inhibitors at high resolution." Crennell S.J., Garman E.F., Philippon C., Vasella A., Laver W.G., Vimr E.R., Taylor G.L. J. Mol. Biol. 259:264-280(1996) [PubMed: 8656428] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). Strain: LT2.
[6]	Garman E.F., Wouters J., Schneider T.R., Vimr E.R., Laver W.G., Sheldrick G.M. Submitted (JUL-1998) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

M55342 Genomic DNA. Translation: AAA27168.1.
AE008737 Genomic DNA. Translation: AAL19864.1. Different initiation.

RefSeq

NP_459905.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DIL	X-ray	1.90	A	1-382	[»]
1DIM	X-ray	1.60	A	1-382	[»]
2SIL	X-ray	1.60	A	1-382	[»]
2SIM	X-ray	1.60	A	1-382	[»]
3SIL	X-ray	1.05	A	4-382	[»]

ModBase

Search...

Genome annotation databases

GeneID

1252447.

GenomeReviews

Gene locus STM0928 in contig AE006468_GR.

KEGG

stm:STM0928.

NMPDR

fig|99287.1.peg.895.

Organism-specific databases

StyGene

nanH. SG10244.

CMR

Search...

Phylogenomic databases

HOGENOM

P29768.

Enzyme and pathway databases

BioCyc

STYP99287:STM0928-MON.

Family and domain databases

InterPro

IPR002860. BNR.
[Graphical view]

Pfam

PF02012. BNR. 4 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P29768.

Entry information

Entry name

NANH_SALTY

Accession

Primary (citable) accession number: P29768

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	November 4, 2008
This is version 73 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)