CAZyme Information: MGYG000000745_00259

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74
• CAZyme ID: MGYG000000745_00259
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
853	MGYG000000745_3|CGC1	94848.52	5.7798

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000745	2615728	MAG	Kazakhstan	Asia

• Gene Location: Start: 53949; End: 56510 Strand: +

Full Sequence      

MSVDYYAVDGYHGGKYGHMPLGAFRDILQKLRENPDWKLSLDIEPVSWDDLKLRDPATYA
QLRQMLMDGQSPRLEIVSATYAQPYPWLTDGESFIRQMRGGLKKTAEHFPFLRVTTYAVQ
EPCWTSALPQLLRSFGFELAVLKNPSTAWAGYCEGAEGEMRTWIGPDGTSIPAVPRYACE
GLLTTWQTESVFARRGFVERCRRSGVARPAGMCFQDLGWPACPYVTQPFFVEYLPEEMLA
KGSVRYTTWKEYAQTIADAPAPAWRVSQEAFRVALPWGDQQLTHMARMVRRGENALLEAQ
WLDTLRFARTGRSAGGVLEQAAEQMMLAQHHDAWICASCGEEEKNWAKVTCARVLSAEHL
LEGACRDALLDLTGPVASAAGPDAQDALLVNTLARAEERLVSVPVTFGRGVRGARVWQGG
IEAPCQFICERAYEDGSWNAGTLLARVRVDGMGTDALRVEPLPEEEKRPPLASATVADDT
ATLENELYRITLDLRRGGAVAAFICKADGRNLVDAASDKPFNGFVGYAIDARKWVSSADT
AATAQAELSGPLAARVRLCGKVGDIPFTQTLTLRAGERALTVEAEFDFPEKTHIGEDFPI
ADENALVERHRSYHDGRYKLNAYFPTAFRQERLFKDAAFDVCESRQADTYFQRWDEIKHN
ILISFVDACDQERGLAVFSDHTTSYIHGADEPLGLTVAWAADGGYWWRNRALSGRHTVRY
AILPHMGDWRAAGLWHEGQKLRHPVLARQAGGLCENAAFTLLRVTHGEAELSETIAEADG
VTLRLFNPGEAETQRLWLSDAFLPEITLCELDGRAVSTLRATRGAQGGLILALPMPRFAV
RSLRLTKKAMKEE

Enzyme Prediction     

No EC number prediction in MGYG000000745_00259.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	24	267	4.4e-22	0.8587360594795539

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0383	AMS1	5.38e-09	545	810	659	912	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10786	GH38N_AMII_like	6.17e-08	16	173	18	172	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.
cd10789	GH38N_AMII_ER_cytosolic	1.57e-07	24	173	29	171	N-terminal catalytic domain of endoplasmic reticulum(ER)/cytosolic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). The subfamily is represented by Saccharomyces cerevisiae vacuolar alpha-mannosidase Ams1, rat ER/cytosolic alpha-mannosidase Man2C1, and similar proteins. Members in this family share high sequence similarity. None of them have any classical signal sequence or membrane spanning domains, which are typical of sorting or targeting signals. Ams1 functions as a second resident vacuolar hydrolase in S. cerevisiae. It aids in recycling macromolecular components of the cell through hydrolysis of terminal, non-reducing alpha-d-mannose residues. Ams1 utilizes both the cytoplasm to vacuole targeting (Cvt, nutrient-rich conditions) and autophagic (starvation conditions) pathways for biosynthetic delivery to the vacuole. Man2C1is involved in oligosaccharide catabolism in both the ER and cytosol. It can catalyze the cobalt-dependent cleavage of alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues. 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.
smart00872	Alpha-mann_mid	2.16e-05	287	339	14	67	Alpha mannosidase, middle domain. Members of this entry belong to the glycosyl hydrolase family 38, This domain, which is found in the central region adopts a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase.
pfam09261	Alpha-mann_mid	2.76e-04	287	367	15	97	Alpha mannosidase middle domain. Members of this family adopt a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. They are predominantly found in the enzyme alpha-mannosidase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDU58944.1	1.74e-153	6	847	29	853
QUR49563.1	2.38e-153	6	848	25	854
BBL06663.1	3.27e-153	6	847	59	880
BBL00893.1	3.46e-153	6	847	61	882
QJE28473.1	4.71e-153	6	848	25	854

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
1.000042	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000745_00259.