CAZyme Information: EPrPIT00000022661-p1

Basic Information

• Species: Globisporangium irregulare
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium irregulare
• CAZyme ID: EPrPIT00000022661-p1
• CAZy Family: GH72
• CAZyme Description: Lysosomal alpha-mannosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1067		121154.89	6.5928

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GirregulareDAOMBR486	13869	1223557	65	13804

• Gene Location: location=PirrDAOMBR486_SC1007:6462-9995(-)

Full Sequence      

MRATRVLAAVPLLKSSERCNASRWTLPVDGKYNTKGEVDPHKLNVHLIAHSHDDPGWLFS
IDQYYMQRVQYTLDTVVEELLEDPNRQFMFVEQRFELTIISPVQSFFQRWWHQQSSETKL
IVKQLVKEGRLDLSVNGGWCMHDEATPHYTAMVDQTAYGHHLLREEFNITPRIGWQIDPF
GHSSTQGSLLSAGVGFDALYFARIDYQDYALRKSKQNLEFIWRPSKSRGKHSQVFTGEII
NHYGPPLEFDFAYRERQIQDDSELHDFNVCSQVDDFVRMAHERGVSTKGNHIFIPMGGDF
QYDNARRWYKNMDKLVHYVNQDNRVSVLYSNLSYYTDLKLAENLTWSVKIDDFFPYASGK
YQYWSGFFTSRPALKRFARVSNTLFQQVRQLHALYQTHHAAQLDKLQRAVGLVQHHDGLS
GTEKQAVADDYALRLNEGILDAEKELNEVFFVIGEKEKYEFCLLANVSTCNVSTSNEQFE
VLVHNALARKSVQTISIPIVFKNVDIQVISGSAKVRQHEVFAAVPVHLDQMAAPYSLVFS
TELDPLSEARFLVSKKTKAGESDSPKPLSAELDIDAQEKITLENDLMRVKIAKDTGSIIS
ITNKKKNIELPLSSRVLYYQSFQAKNNQRSGAYIFRPDSKTVHPVAGKADKVRLIDLQVD
GAASGGTASRVAFQIGKWVTLEYRVNADDEFVEIEWTVGSIPIGDKKGKEVIIRFNSQKS
IKSAKTLYTDSNGLEFISRVRNHRDTWNLKLHDDTEFVAANYFPITTGAYIKDDKYQLNI
VTDRAQGAASLEDGQIEVMVHRRLLADDSKGVGEFLNETESFFDKLTQKETTRGLIVRGN
FFINVDSATEGIRSIRTKMERQLFAPLVAFRKLSKTEVDGAKVPWLAVTDFPENVGLTTL
QRLSRDCLMARLTHLYSVEEHASLSKPVKVDFSKLFTVQNATISDVSELLLTGIASLNSQ
AREPYAAKWKTSELEDPEKLDYDCKASTPLNGGTEVELQAMEVRSFRVCFKKSTEKQAAE
YTSGRATGNDDADMKRDFRVVTGEEADLKLTGSAPHLAEMDEIMAVQ

Enzyme Prediction     

EC	3.2.1.24:47	3.2.1.113:25	3.2.1.114:7

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	44	357	6.9e-67	0.9962825278810409

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
212121	GH38N_AMII_LAM_like	1.13e-146	43	321	1	278	N-terminal catalytic domain of lysosomal alpha-mannosidase and similar proteins; glycoside hydrolase family 38 (GH38). The subfamily is represented by lysosomal alpha-mannosidase (LAM, Man2B1, EC 3.2.1.114), which is a broad specificity exoglycosidase hydrolyzing all known alpha 1,2-, alpha 1,3-, and alpha 1,6-mannosidic linkages from numerous high mannose type oligosaccharides. LAM is expressed in all tissues and in many species. In mammals, the absence of LAM can cause the autosomal recessive disease alpha-mannosidosis. LAM has an acidic pH optimum at 4.0-4.5. It is stimulated by zinc ion and is inhibited by cobalt ion and plant alkaloids, such as swainsonine (SW). LAM catalyzes hydrolysis by a double displacement mechanism in which a glycosyl-enzyme intermediate is formed and hydrolyzed via oxacarbenium ion-like transition states. A carboxylic acid in the active site acts as the catalytic nucleophile in the formation of the covalent intermediate while a second carboxylic acid acts as a general acid catalyst. The same residue is thought to assist in the hydrolysis (deglycosylation) step, this time acting as a general base.
212095	GH38N_AMII_euk	6.12e-98	43	320	1	257	N-terminal catalytic domain of eukaryotic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). The family corresponds to a group of eukaryotic class II alpha-mannosidases (AlphaMII), which contain Golgi alpha-mannosidases II (GMII), the major broad specificity lysosomal alpha-mannosidases (LAM, MAN2B1), the noval core-specific lysosomal alpha 1,6-mannosidases (Epman, MAN2B2), and similar proteins. GMII catalyzes the hydrolysis of the terminal both alpha-1,3-linked and alpha-1,6-linked mannoses from the high-mannose oligosaccharide GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2 (GlcNAc, N-acetylglucosmine), which is the committed step of complex N-glycan synthesis. LAM is a broad specificity exoglycosidase hydrolyzing all known alpha 1,2-, alpha 1,3-, and alpha 1,6-mannosidic linkages from numerous high mannose type oligosaccharides. Different from LAM, Epman can efficiently cleave only the alpha 1,6-linked mannose residue from (Man)3GlcNAc, but not (Man)3(GlcNAc)2 or other larger high mannose oligosaccharides, in the core of N-linked glycans. Members in this family are retaining glycosyl hydrolases of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. Two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst.
395852	Glyco_hydro_38	4.00e-83	44	357	1	271	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
178304	PLN02701	2.85e-77	37	814	34	858	alpha-mannosidase
212120	GH38N_AMII_GMII_SfManIII_like	3.06e-70	42	368	1	340	N-terminal catalytic domain of Golgi alpha-mannosidase II, Spodoptera frugiperda Sf9 alpha-mannosidase III, and similar proteins; glycoside hydrolase family 38 (GH38). This subfamily is represented by Golgi alpha-mannosidase II (GMII, also known as mannosyl-oligosaccharide 1,3- 1,6-alpha mannosidase, EC 3.2.1.114, Man2A1), a monomeric, membrane-anchored class II alpha-mannosidase existing in the Golgi apparatus of eukaryotes. GMII plays a key role in the N-glycosylation pathway. It catalyzes the hydrolysis of the terminal both alpha-1,3-linked and alpha-1,6-linked mannoses from the high-mannose oligosaccharide GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2(GlcNAc, N-acetylglucosmine), which is the committed step of complex N-glycan synthesis. GMII is activated by zinc or cobalt ions and is strongly inhibited by swainsonine. Inhibition of GMII provides a route to block cancer-induced changes in cell surface oligosaccharide structures. GMII has a pH optimum of 5.5-6.0, which is intermediate between those of acidic (lysosomal alpha-mannosidase) and neutral (ER/cytosolic alpha-mannosidase) enzymes. GMII is a retaining glycosyl hydrolase of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl enzyme complex; two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst. This subfamily also includes human alpha-mannosidase 2x (MX, also known as mannosyl-oligosaccharide 1,3- 1,6-alpha mannosidase, EC 3.2.1.114, Man2A2). MX is enzymatically and functionally very similar to GMII, and is thought to also function in the N-glycosylation pathway. Also found in this subfamily is class II alpha-mannosidase encoded by Spodoptera frugiperda Sf9 cell. This alpha-mannosidase is an integral membrane glycoprotein localized in the Golgi apparatus. It shows high sequence homology with mammalian Golgi alpha-mannosidase II(GMII). It can hydrolyze p-nitrophenyl alpha-D-mannopyranoside (pNP-alpha-Man), and it is inhibited by swainsonine. However, the Sf9 enzyme is stimulated by cobalt and can hydrolyze (Man)5(GlcNAc)2 to (Man)3(GlcNAc)2, but it cannot hydrolyze GlcNAc(Man)5(GlcNAc)2, which is distinct from that of GMII. Thus, this enzyme has been designated as Sf9 alpha-mannosidase III (SfManIII). It probably functions in an alternate N-glycan processing pathway in Sf9 cells.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ27314.1|GH38	0.0	66	1012	1	950
CCA13903.1|GH38	0.0	19	1013	23	1009
AIG56315.1|GH38	2.37e-292	1	1034	1	954
AIG56101.1|GH38	4.77e-249	3	1014	4	962
QHN98206.1|GH38	6.63e-209	31	1011	35	1014

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6B9O_A	1.00e-201	31	1010	2	981	Structure of GH 38 Jack Bean alpha-mannosidase [Canavalia ensiformis],6B9O_B Structure of GH 38 Jack Bean alpha-mannosidase [Canavalia ensiformis]
6B9P_A	1.00e-201	31	1010	2	981	Structure of GH 38 Jack Bean alpha-mannosidase in complex with a 36-valent iminosugar cluster inhibitor [Canavalia ensiformis],6B9P_B Structure of GH 38 Jack Bean alpha-mannosidase in complex with a 36-valent iminosugar cluster inhibitor [Canavalia ensiformis]
1O7D_A	7.71e-73	32	326	3	297	The structure of the bovine lysosomal a-mannosidase suggests a novel mechanism for low pH activation [Bos taurus]
1HWW_A	2.20e-62	24	814	36	850	GOLGI ALPHA-MANNOSIDASE II IN COMPLEX WITH SWAINSONINE [Drosophila melanogaster],1HXK_A Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin [Drosophila melanogaster]
6RPC_A	2.50e-62	24	814	54	868	Chain A, Alpha-mannosidase 2 [Drosophila melanogaster],6RQZ_A Chain A, Alpha-mannosidase 2 [Drosophila melanogaster],6RRH_A Chain A, Alpha-mannosidase 2 [Drosophila melanogaster],6RRJ_A Chain A, Alpha-mannosidase 2 [Drosophila melanogaster],6RRN_A Chain A, Alpha-mannosidase 2 [Drosophila melanogaster],6RRU_A Chain A, Alpha-mannosidase 2 [Drosophila melanogaster],6RRW_A Chain A, Alpha-mannosidase 2 [Drosophila melanogaster],6RRX_A Chain A, Alpha-mannosidase 2 [Drosophila melanogaster],6RRY_A Chain A, Alpha-mannosidase 2 [Drosophila melanogaster],6RS0_A Chain A, Alpha-mannosidase 2 [Drosophila melanogaster]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8LPJ3|MANA2_ARATH	4.06e-206	32	1005	26	1005	Probable alpha-mannosidase At5g13980 OS=Arabidopsis thaliana OX=3702 GN=At5g13980 PE=2 SV=1
sp|P94078|MANA1_ARATH	6.71e-199	31	1015	26	1008	Alpha-mannosidase At3g26720 OS=Arabidopsis thaliana OX=3702 GN=At3g26720 PE=1 SV=1
sp|Q9FKW9|MANA3_ARATH	2.73e-195	31	1010	35	1035	Probable alpha-mannosidase At5g66150 OS=Arabidopsis thaliana OX=3702 GN=At5g66150 PE=3 SV=1
sp|C0HJB3|MANA_CANEN	9.80e-194	31	1010	2	981	Alpha-mannosidase OS=Canavalia ensiformis OX=3823 PE=1 SV=1
sp|Q8VHC8|MA2B1_CAVPO	1.03e-181	32	1006	50	997	Lysosomal alpha-mannosidase OS=Cavia porcellus OX=10141 GN=MAN2B1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000060	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EPrPIT00000022661-p1.