CAZyme Information: MGYG000001525_03997

Basic Information

• Species: Paenibacillus_A rubinfantis
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A rubinfantis
• CAZyme ID: MGYG000001525_03997
• CAZy Family: GH0
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
820	MGYG000001525_20|CGC10	93988.16	5.4044

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001525	5369528	Isolate	not provided	not provided

• Gene Location: Start: 505961; End: 508423 Strand: -

Full Sequence      

MKLSKKWKVFLVHHSHTDIGYTERQDKIIHYHSDFIKQAIDILREADRTGNQARKGFVWQ
CENHWQVKNFYDHAPSDYITDFEKYVRAGRIGLSGNYMNLTELVSRDILYDCTIQAKVYG
EQIGFPVRSGMSADINGFAWGYADVLQECGVERLFSCLHSHHGMFPLYKKQTPFYWQGPS
GKKVLVWNGEHYHFGNEFCFSPHAASTYMIFDEISKKMRGNQLFTTSPEDTEQVELAILE
ERLERYLQNLEAEGYPGDFVPFMVSGAITDNAPPNVKIAERVDWLNRKYAGTLEVCMATL
DQFFDHLEANWKDIPVYQGDWNDWWADGVGSTPAVVKVYREGQRKYDLCKKLDPDSALGD
AGLMQKAAENLILYSEHTWGYSSSVSEPWETLVGELEHKKSAYAINGNTEAADNLDRILA
KKGEVAIRQDRPQHYRIINPHDLPLETTAKVYIEFWEYINGLNYSLDIPIEVVDLATNEV
ISHQVKRIARAYEIEIPLKLQPKEERNVGVRATGQYRNGTSQNHAHIGAEGVEDVLQPGA
PREDVACVETTFYRVELDQKRGITSIIDRKSGKNLVRQGAAYAPFSGIYEVTDIRTSPTE
ERRRMGRNRKSPATRRYEARLTDIQIVESGPLFVSLQLDYSLEGTRFYMVFLKLYREINK
IEAMVRVHKDSVWDPENLYVSLPFTAGDDEVKYVDKTGCILRPGIDQLPGSNMEFYLIQN
GLVMEAGERQVLVAVKDTPLLTFGPLEAKPIQLCDGNNWELNRGETFAWVMNNYWETNFK
VDLGGFYEFAFTLSCQDKQTTEAAMRLCEAYNEGLLAFYI

Enzyme Prediction     

No EC number prediction in MGYG000001525_03997.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	1.87e-74	8	286	1	253	N-terminal catalytic domain of mainly uncharacterized eukaryotic proteins similar to alpha-mannosidases; glycoside hydrolase family 38 (GH38). The subfamily of mainly uncharacterized eukaryotic proteins shows sequence homology with class II alpha-mannosidases (AlphaAMIIs). AlphaAMIIs possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyze the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. This subfamily belongs to the GH38 family of retaining glycosyl hydrolases, which employ 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.
pfam01074	Glyco_hydro_38	1.14e-11	8	317	1	270	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10786	GH38N_AMII_like	5.67e-10	8	252	1	251	N-terminal catalytic domain of class II alpha-mannosidases and similar proteins; glycoside hydrolase family 38 (GH38). Alpha-mannosidases (EC 3.2.1.24) are extensively found in eukaryotes and play important roles in the processing of newly formed N-glycans and in degradation of mature glycoproteins. A deficiency of this enzyme causes the lysosomal storage disease alpha-mannosidosis. Many bacterial and archaeal species also possess putative alpha-mannosidases, but their activity and specificity is largely unknown. Based on different functional characteristics and sequence homology, alpha-mannosidases have been organized into two classes (class I, belonging to glycoside hydrolase family 47, and class II, belonging to glycoside hydrolase family 38). Members of this family corresponds to class II alpha-mannosidases (alphaMII), which contain intermediate Golgi alpha-mannosidases II, acidic lysosomal alpha-mannosidases, animal sperm and epididymal alpha -mannosidases, neutral ER/cytosolic alpha-mannosidases, and some putative prokaryotic alpha-mannosidases. AlphaMII possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyzes the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANS75706.1	0.0	1	820	1	820
SET75050.1	0.0	1	819	1	818
AUS96542.1	0.0	2	820	13	830
QDA73873.1	1.80e-278	1	820	1	809
QPJ27012.1	4.13e-277	1	820	1	809

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000057	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001525_03997.