CAZyme Information: MGYG000002282_00164

Basic Information

• Species: Parabacteroides gordonii
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides gordonii
• CAZyme ID: MGYG000002282_00164
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
975	MGYG000002282_1|CGC4	110447.16	6.2625

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002282	6348794	Isolate	China	Asia

• Gene Location: Start: 218483; End: 221410 Strand: +

Full Sequence      

MNVVDFKLNTMKKRIAYCLFASVLSSMIYADVVPSTIDYVVRPLYGYRADGTPGRIVTVK
LKGKELKGDLSVDVITKGKTEKNHFVLNAKDSTEVEVLLPPTVPAGKKSEVTFVLSSAGK
KEKQKVSISPMRQWNVYLYNHSHVDIGYTNTHKNVERLHKTNIIEGVRLAEETKNHPEGS
RYVWNPEIGWPLERLWQSEPERREALIGAVKKGQLCVDASYLNLNTSTCSDEELFHVFKF
TREIQRLSGVPSDVFQQFDIPGVSWGLIPVMAQEGVKYIISWPNSDRAGNAHKYQMDGRP
FWWIGPDGESKVLFFQPGGYANSGSMGKGRTTGRPWFGQRDPEKVPAVIRTGEADVDFTR
QLTEMEAENYPYDFAVFSWTLWDNCPLDADIPYAVKAWNEKYAYPKIKICGGHEIMSMIE
EKYGDRLPVVTGDYTEYWTDGLGTAAGLTAMNRNAKERLLQAETIWSMLANGTKAPRYDF
DEAWRYILLGSEHTWCFENPTEPYFQDAIWKVKQSYFHEAEDRSIDMLDESLAPVTDKSD
GALGPKEGPSNGGIAVFNTHTWPKSGVITLSSKESLKGDKVVDQDGKEVLSQRLSSGELL
FYASEVPALGSRHYRVVEGKCTLSSRCRINGNTLENEYLTVRLDPVTGNIVYLAKNGSEY
NYVNRGANTFSWLPANVDAPQADTVESVSVVEEGPLAVELRITSKATGCRSVSRSVRLQA
GQPWVEISNIVDKLPLVEKDGIHFGFDFNLPDSKTRVDIPWGMMEVEKDQWPQGNRNWLA
MQRWLDVSNSTHGVTWCSLDAPLFEYGDRYANISMSWGGQGNWITKLEPSSTIYSWVMNN
HWHTNFPLTQDGPVRFRYRLYPHEEYNVVEANRFGLEQSQPLVYATADKARVIKPVITID
NERVYTTILKSTDKDKELIVRLRSLSDKAEPVKLFFPKADPKSLMICEREEIPVKPTNGE
FMMKPYGQITLKIEY

Enzyme Prediction     

No EC number prediction in MGYG000002282_00164.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	1.71e-76	136	400	2	254	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.
pfam07748	Glyco_hydro_38C	2.35e-13	634	795	1	174	Glycosyl hydrolases family 38 C-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10786	GH38N_AMII_like	1.78e-12	135	322	1	181	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.
COG0383	AMS1	2.63e-07	444	975	456	943	Alpha-mannosidase [Carbohydrate transport and metabolism].
pfam01074	Glyco_hydro_38	1.86e-06	135	320	1	179	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SDS34905.1	0.0	32	974	45	990
AOW10592.1	0.0	6	975	5	968
AOW10591.1	0.0	6	975	5	970
AUN37913.1	0.0	13	975	10	968
AUN37912.1	0.0	280	975	1	692

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
0.000562	0.998631	0.000212	0.000197	0.000191	0.000174

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002282_00164.