DB code: M00310

CATH domain	-.-.-.- :
	3.30.750.60 : Transcription Regulator spoIIAA
	2.120.10.10 : Neuraminidase	Catalytic domain
	2.40.30.20 : Elongation Factor Tu (Ef-tu); domain 3
	4.10.1090.10 : Endosialidase, domain 4
	-.-.-.- :
	2.-.-.- :
	1.-.-.- :
E.C.	3.2.1.129
CSA	1v0e
M-CSA	1v0e
MACiE

CATH domain	Related DB codes (homologues)
2.120.10.10 : Neuraminidase	D00173 T00064 T00065 T00208

Uniprot Enzyme Name
UniprotKB	Protein name	Synonyms	RefSeq	CAZy	MEROPS	Pfam
Q858B1		Endo-N-acetylneuraminidase Endo-alpha-sialidase EC 3.2.1.129 Precursor of gp17 EC 3.2.1.129	YP_338127.1 (Protein) NC_007456.1 (DNA/RNA sequence)	GH58 (Glycoside Hydrolase Family 58)	S74.001 (Serine)	PF12195 (End_beta_barrel) PF12217 (End_beta_propel) PF12218 (End_N_terminal) PF12219 (End_tail_spike) PF03906 (Phage_T7_tail) [Graphical View]
Q04830	Endo-N-acetylneuraminidase	Endo-N EC 3.2.1.129 Endosialidase G102		GH58 (Glycoside Hydrolase Family 58)		PF12195 (End_beta_barrel) PF12217 (End_beta_propel) PF12218 (End_N_terminal) PF12219 (End_tail_spike) PF03906 (Phage_T7_tail) [Graphical View]

KEGG enzyme name
Endo-alpha-sialidase Endo-N-acylneuraminidase Endoneuraminidase Endo-N-acetylneuraminidase Poly(alpha-2,8-sialosyl) endo-N-acetylneuraminidase Poly(alpha-2,8-sialoside) alpha-2,8-sialosylhydrolase Endosialidase Endo-N

UniprotKB: Accession Number	Entry name	Activity	Subunit	Subcellular location	Cofactor
Q858B1	Q858B1_BPK1F	Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or poly(sialic) acids.	Homotrimer.
Q04830	ENAN_BPK1F	Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or poly(sialic) acids.	Homotrimer.

KEGG Pathways
Map code	Pathways	E.C.

Compound table
						Substrates		Products		Intermediates
KEGG-id						C04466	C00001	L00073	C04466
E.C.
Compound						alpha-2,8-Linked polymer of sialic acid	H2O	beta-sialic acid at reducing end of alpha-2,8-Linked polymer of sialic acid	alpha-2,8-Linked polymer of sialic acid
Type						amide group,carboxyl group,polysaccharide	H2O	amide group,carboxyl group,polysaccharide	amide group,carboxyl group,polysaccharide
ChEBI							15377 15377
PubChem							22247451 962 22247451 962
1v0eA01						Unbound		Unbound	Unbound
1v0eB01						Unbound		Unbound	Unbound
1v0eC01						Unbound		Unbound	Unbound
1v0eD01						Unbound		Unbound	Unbound
1v0eE01						Unbound		Unbound	Unbound
1v0eF01						Unbound		Unbound	Unbound
1v0fA01						Unbound		Unbound	Unbound
1v0fB01						Unbound		Unbound	Unbound
1v0fC01						Unbound		Unbound	Unbound
1v0fD01						Unbound		Unbound	Unbound
1v0fE01						Unbound		Unbound	Unbound
1v0fF01						Unbound		Unbound	Unbound
3gvjA01						Unbound		Unbound	Unbound
3gvkA01						Unbound		Unbound	Unbound
3gvkB01						Unbound		Unbound	Unbound
3gvkC01						Unbound		Unbound	Unbound
3gvlA01						Unbound		Unbound	Unbound
3ju4A01						Unbound		Unbound	Unbound
1v0eA02						Unbound		Unbound	Unbound
1v0eB02						Unbound		Unbound	Unbound
1v0eC02						Unbound		Unbound	Unbound
1v0eD02						Unbound		Unbound	Unbound
1v0eE02						Unbound		Unbound	Unbound
1v0eF02						Unbound		Unbound	Unbound
1v0fA02						Unbound		Unbound	Unbound
1v0fB02						Unbound		Unbound	Unbound
1v0fC02						Unbound		Unbound	Unbound
1v0fD02						Unbound		Unbound	Unbound
1v0fE02						Unbound		Unbound	Unbound
1v0fF02						Unbound		Unbound	Unbound
3gvjA02						Unbound		Unbound	Unbound
3gvkA02						Unbound		Bound:SLB-SIA-SIA	Unbound
3gvkB02						Unbound		Bound:SLB-SIA-SIA	Unbound
3gvkC02						Unbound		Bound:SLB-SIA-SIA	Unbound
3gvlA02						Unbound		Unbound	Unbound
3ju4A02						Unbound		Unbound	Unbound
1v0eA03						Unbound		Unbound	Unbound
1v0eB03						Unbound		Unbound	Unbound
1v0eC03						Unbound		Unbound	Unbound
1v0eD03						Unbound		Unbound	Unbound
1v0eE03						Unbound		Unbound	Unbound
1v0eF03						Unbound		Unbound	Unbound
1v0fA03						Unbound		Unbound	Unbound
1v0fB03						Unbound		Unbound	Unbound
1v0fC03						Unbound		Unbound	Unbound
1v0fD03						Unbound		Unbound	Unbound
1v0fE03						Unbound		Unbound	Unbound
1v0fF03						Unbound		Unbound	Unbound
3gvjA03						Unbound		Unbound	Unbound
3gvkA03						Unbound		Unbound	Unbound
3gvkB03						Unbound		Unbound	Unbound
3gvkC03						Unbound		Unbound	Unbound
3gvlA03						Unbound		Unbound	Unbound
3ju4A03						Unbound		Unbound	Unbound
1v0eA04						Unbound		Unbound	Unbound
1v0eB04						Unbound		Unbound	Unbound
1v0eC04						Unbound		Unbound	Unbound
1v0eD04						Unbound		Unbound	Unbound
1v0eE04						Unbound		Unbound	Unbound
1v0eF04						Unbound		Unbound	Unbound
1v0fA04						Unbound		Unbound	Unbound
1v0fB04						Unbound		Unbound	Unbound
1v0fC04						Unbound		Unbound	Unbound
1v0fD04						Unbound		Unbound	Unbound
1v0fE04						Unbound		Unbound	Unbound
1v0fF04						Unbound		Unbound	Unbound
3gvjA04						Unbound		Unbound	Unbound
3gvkA04						Unbound		Unbound	Unbound
3gvkB04						Unbound		Unbound	Unbound
3gvkC04						Unbound		Unbound	Unbound
3gvlA04						Unbound		Unbound	Unbound
3ju4A04						Unbound		Unbound	Unbound
3gw6A01						Unbound		Unbound	Unbound
3gw6B01						Unbound		Unbound	Unbound
3gw6C01						Unbound		Unbound	Unbound
3gw6D01						Unbound		Unbound	Unbound
3gw6E01						Unbound		Unbound	Unbound
3gw6F01						Unbound		Unbound	Unbound
3gw6A02						Unbound		Unbound	Unbound
3gw6B02						Unbound		Unbound	Unbound
3gw6C02						Unbound		Unbound	Unbound
3gw6D02						Unbound		Unbound	Unbound
3gw6E02						Unbound		Unbound	Unbound
3gw6F02						Unbound		Unbound	Unbound
3gw6A03						Unbound		Unbound	Unbound
3gw6B03						Unbound		Unbound	Unbound
3gw6C03						Unbound		Unbound	Unbound
3gw6D03						Unbound		Unbound	Unbound
3gw6E03						Unbound		Unbound	Unbound
3gw6F03						Unbound		Unbound	Unbound
3gw6A04						Unbound		Unbound	Unbound
3gw6B04						Unbound		Unbound	Unbound
3gw6C04						Unbound		Unbound	Unbound
3gw6D04						Unbound		Unbound	Unbound
3gw6E04						Unbound		Unbound	Unbound
3gw6F04						Unbound		Unbound	Unbound

Reference for Active-site residues
resource	references	E.C.
Literature [6]

Active-site residues
PDB						Catalytic residues	Cofactor-binding residues	Modified residues	Main-chain involved in catalysis	Comment
1v0eA01
1v0eB01
1v0eC01
1v0eD01
1v0eE01
1v0eF01
1v0fA01
1v0fB01
1v0fC01
1v0fD01
1v0fE01
1v0fF01
3gvjA01
3gvkA01
3gvkB01
3gvkC01
3gvlA01
3ju4A01
1v0eA02						HIS 350;GLU 581;ARG 596;ARG 647
1v0eB02						HIS 350;GLU 581;ARG 596;ARG 647
1v0eC02						HIS 350;GLU 581;ARG 596;ARG 647
1v0eD02						HIS 350;GLU 581;ARG 596;ARG 647
1v0eE02						HIS 350;GLU 581;ARG 596;ARG 647
1v0eF02						HIS 350;GLU 581;ARG 596;ARG 647
1v0fA02						HIS 350;GLU 581;ARG 596;ARG 647
1v0fB02						HIS 350;GLU 581;ARG 596;ARG 647
1v0fC02						HIS 350;GLU 581;ARG 596;ARG 647
1v0fD02						HIS 350;GLU 581;ARG 596;ARG 647
1v0fE02						HIS 350;GLU 581;ARG 596;ARG 647
1v0fF02						HIS 350;GLU 581;ARG 596;ARG 647
3gvjA02						HIS 350;GLU 581;ARG 596;				mutant R647A
3gvkA02						;GLU 581;ARG 596;ARG 647				mutant H350A
3gvkB02						;GLU 581;ARG 596;ARG 647				mutant H350A
3gvkC02						;GLU 581;ARG 596;ARG 647				mutant H350A
3gvlA02						HIS 350;GLU 581;ARG 596;ARG 647
3ju4A02						HIS 350;GLU 581;ARG 596;ARG 647
1v0eA03
1v0eB03
1v0eC03
1v0eD03
1v0eE03
1v0eF03
1v0fA03
1v0fB03
1v0fC03
1v0fD03
1v0fE03
1v0fF03
3gvjA03
3gvkA03
3gvkB03
3gvkC03
3gvlA03
3ju4A03
1v0eA04
1v0eB04
1v0eC04
1v0eD04
1v0eE04
1v0eF04
1v0fA04
1v0fB04
1v0fC04
1v0fD04
1v0fE04
1v0fF04
3gvjA04
3gvkA04
3gvkB04
3gvkC04
3gvlA04
3ju4A04
3gw6A01
3gw6B01
3gw6C01
3gw6D01
3gw6E01
3gw6F01
3gw6A02
3gw6B02
3gw6C02
3gw6D02
3gw6E02
3gw6F02
3gw6A03
3gw6B03
3gw6C03
3gw6D03
3gw6E03
3gw6F03
3gw6A04
3gw6B04
3gw6C04
3gw6D04
3gw6E04
3gw6F04

References for Catalytic Mechanism
References	Sections	No. of steps in catalysis
[6]	Fig.3, Fig.4, p.347-348

References
[1]
Resource
Comments
Medline ID
PubMed ID	15608653
Journal	Nat Struct Mol Biol
Year	2005
Volume	12
Pages	90-6
Authors	Stummeyer K, Dickmanns A, Muhlenhoff M, Gerardy-Schahn R, Ficner R
Title	Crystal structure of the polysialic acid-degrading endosialidase of bacteriophage K1F.
Related PDB	1v0e 1v0f
Related UniProtKB	Q858B1
[2]
Resource
Comments
Medline ID
PubMed ID	16991177
Journal	Chembiochem
Year	2006
Volume	7
Pages	1875-7
Authors	Haselhorst T, Stummeyer K, Muhlenhoff M, Schaper W, Gerardy-Schahn R, von Itzstein M
Title	Endosialidase NF appears to bind polySia DP5 in a helical conformation.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID	18558099
Journal	Curr Opin Chem Biol
Year	2008
Volume	12
Pages	539-55
Authors	Vocadlo DJ, Davies GJ
Title	Mechanistic insights into glycosidase chemistry.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID	19411257
Journal	J Biol Chem
Year	2009
Volume	284
Pages	17404-10
Authors	Morley TJ, Willis LM, Whitfield C, Wakarchuk WW, Withers SG
Title	A new sialidase mechanism: bacteriophage K1F endo-sialidase is an inverting glycosidase.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID	20124697
Journal	Acta Crystallogr D Biol Crystallogr
Year	2010
Volume	66
Pages	176-80
Authors	Schulz EC, Neumann P, Gerardy-Schahn R, Sheldrick GM, Ficner R
Title	Structure analysis of endosialidase NF at 0.98 A resolution.
Related PDB	3ju4
Related UniProtKB	Q04830
[6]
Resource
Comments
Medline ID
PubMed ID	20096705
Journal	J Mol Biol
Year	2010
Volume	397
Pages	341-351
Authors	Schulz EC, Schwarzer D, Frank M, Stummeyer K, Muhlenhoff M, Dickmanns A, Gerardy-Schahn R, Ficner R
Title	Structural Basis for the Recognition and Cleavage of Polysialic Acid by the Bacteriophage K1F Tailspike Protein EndoNF.
Related PDB	3gvj 3gvk 3gvl
Related UniProtKB	Q858B1

Comments

This enzyme belongs to glycosidase family-58, with an inverting mechanism. According to the literature [6], His350 seems to act as a general acid to protonate the leaving group in the SN1-like reaction. On the other hand, it is not still cleare which group can act as a general base to activate the hydrolytic water, substrate carboxylate or Glu581. Moreover, Arg596 and Arg647 may be involved in catalysis.

Created	Updated
2010-04-13	2012-02-20