CAZyme Information: MGYG000002592_02090

Basic Information

• Species: Alistipes sp902388705
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp902388705
• CAZyme ID: MGYG000002592_02090
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1148	MGYG000002592_59|CGC1	128449.01	6.3884

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002592	2965227	MAG	China	Asia

• Gene Location: Start: 8536; End: 11982 Strand: +

Full Sequence      

MKKTRILILTILAALTCTGLRAGTYRHPVWEIGRKDGSAAEFALYDGAYSDLTRKFPGAL
AACEAGHSTPAEIPYILPGPQDGWAGNNRGTLLLRFGADRQAPQAAMRLTLYLVESQAAS
PATLEIQAGDFRTTVRAPKGENTDFPDNKRTTARDLKIEADIPAGTFRAGENMLTIRNIA
GSWIVLDAIVLEADRSVKCVRPGDGACIVGSESKPGLVYGRTKEELRHPVTVSLINWGKP
RRASWSYDGTPGGTVELARGMNTVEMNIPEGYAGRTVKLEVRPQRGETLSTEVKIAPAAK
WTLYLVQHTHTDIGYTKPQTEILTEHLRYIDYAVEYCDLTADYPEDAKFRWTCEASWPVR
EWLRIRPQEQVDKFIKYVKAGQIEVTAMFFNMSELSGENNYKTFLEPVTRFRELGLPIET
AMQNDVNGIAWCLADYLPDLGVKYFSIGSNNHRALIPFDRPTLYRWESPSGKGMLMFRGD
HYHTGNSWGIQTGDMARVSNGIFAYIDRLEKSGYPFPLIAVQYSGYLTDNSPPSMRECDL
IRAWNDRYAWPKLRSATSHEFLERIDREHGGELPVYRAAYPDWWTDGFGSAARETAASRK
TQSDLITIEGMLSMAGMAGLGQTDGTHDELRRIHENLLFYDEHTFGAAESIRNPGCENSQ
VQWAEKGSYAWEALKSTQLLYEDAAGRLQGKLYRSTHPTLTLFNPLGWQRSELTTVYIDF
ELIPEGRAFRIVDAEGKSLPVQPIRSRREGRYYAIWAENIPAMGYKTFEIVLDPGKAAEP
QRSELAGNSLENDFYRIGFDPATGTVSSLYDKQLKEELVDPASQWKLGAFIYESLNGDRN
QMERKVFDNYRRSTLSNVRCPGVTSGEIYRSVRFSGKAEGCDERPGVQLEIRLYNDVKRV
EFCYDFVRKPETDPSAIYVAMPWLLEGGELIFDVPGGTVRSGTDQIPGTSASWNTVQNFV
AARNDRAQILVSSDAVPLYLLGKLLDDPYRQPRTYEKPHVFPWLMNNYWTTNFRASQEGE
FKCSFVVSSTADTANSAASRFGWSTRVPLYARVMPAATAANGQQRERSFLRTGCDHVLIT
SCTPTASGEGILLNLRETDGQAATFSLLDAGGRALPIETADATGRVLNEGKVTALTLKPY
ENRFVIVK

Enzyme Prediction     

No EC number prediction in MGYG000002592_02090.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	303	570	1.4e-18	0.9405204460966543

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	1.82e-85	302	545	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	9.36e-41	302	577	1	271	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
PRK09819	PRK09819	1.41e-14	699	815	385	513	mannosylglycerate hydrolase.
pfam07748	Glyco_hydro_38C	4.13e-13	790	945	1	147	Glycosyl hydrolases family 38 C-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10786	GH38N_AMII_like	8.34e-11	302	510	1	204	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
BBL02110.1	0.0	1	1148	1	1147
BBL10048.1	0.0	1	1148	1	1147
BBL12841.1	0.0	1	1148	1	1147
BBL07455.1	0.0	1	1145	1	1145
ALJ40506.1	0.0	5	1148	3	1139

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.001333	0.658294	0.339434	0.000357	0.000292	0.000261

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002592_02090.