CAZyme Information: MGYG000001205_01748

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Gemmiger
• CAZyme ID: MGYG000001205_01748
• CAZy Family: GH0
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
793		89423.32	6.2136

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001205	2359919	MAG	Austria	Europe

• Gene Location: Start: 2217; End: 4598 Strand: +

Full Sequence      

MPRQIKTLYVIHHSHTDIGYTDLQERVVQVQVDYIRSALRILGQARNAAFRWNCETWFCA
EQFLKEAAPAEAEQFFALMRAGRLGFSANYLNFCDLADCAVLDRRLGEACALLRSRGVEP
KTAMCADINGISMGQRDVLLRHGIEFLYTNIHCHHGMYPLYRNQTAYWWENAAGQRLLVW
NGEHYNLGNVLGLRPNRTANFMMQNFGADLPADPVEALRRNLDHYLDECEQNSYPYDFIL
ASVSGVFSDNAPPEPEILRTIEGYAARYPDGVDIRMVSLQELYAAIAPKLQESPVYRGDL
TDWWANGVGSAPYAVKHYREAQHRYALARRLDPAAGEKYPALCREAEDALLLYAEHTWGH
SSTITDPCDTMVLDLDMRKNSYASKAHEAASRLLGAVTREKGDTLRYYNTSGTLRVLAPG
GAPGPQPVEFYVETLSLPRACVRREDGTELPCQVSPHPRGRRITFLDDFTGVCERRYTFA
ERPPLPETLNSRRCYVGAERVRDIVNDYDPVSFRLPYGYENRWFRLDCRAGDGVTALVDK
RCGKNLLGPGAAPFFTPLYEVTPLRPGQTDAYEERRLLGRNIRGPHAVLTAGRLTEVRCE
EHGPVFTRLRLVYALPGTVRADVSVTLYEAVPRIDFALQLGKTLSSDIESVFLPLTLELG
GAQALWAEKGSEPYRPGLDQLPGTCMEYTMSDTGIAFVGEGGSALIASRDVPLYYFGEMR
AHPIRLCENKPEDNHRPVYSWVMNNCWETNFKLDLSGFAEYRYTLWLSAETDPRRAMAEL
TARSFDACAVITG

Enzyme Prediction     

No EC number prediction in MGYG000001205_01748.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	1.87e-70	7	262	1	250	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.
cd10786	GH38N_AMII_like	1.16e-07	7	214	1	207	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.
cd00451	GH38N_AMII_euk	0.009	6	86	1	80	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUI22181.1	3.03e-310	1	768	1	774
QUH31286.1	7.09e-278	7	785	7	787
QUL56909.1	5.74e-163	7	780	8	800
AIQ42834.1	4.97e-161	8	780	9	800
QDH23118.1	1.13e-158	8	772	29	814

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 MGYG000001205_01748.