CAZyme Information: MGYG000002061_00949

Basic Information

• Species: QAMX01 sp004555605
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; QAMX01; QAMX01; QAMX01 sp004555605
• CAZyme ID: MGYG000002061_00949
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
811	MGYG000002061_21|CGC1	89461.94	4.6051

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002061	2191757	MAG	China	Asia

• Gene Location: Start: 15110; End: 17545 Strand: -

Full Sequence      

MKDHPNLYILTYDHGGFVLWKDKVETTLREHIGWLEQYPGFKFGLDYEAFTFDELSKTNP
EIMDLIRDALSKYPGRFGLGSTTYGQPLALFISGESNVRQLTYAIRANRKHFGQTPPVYA
ISEFALISQSPQLLNLCGFEAAILRTHVMNYGYQRTFDAAFGSWIGKDGSAIPAVPAYDD
EGRGFCNTTLDNWILSRWPDDTAISLEDFEAQFRKYQPLLASRYDDLTQPYEKVVADAVQ
HKDWAFVLLEELPGIYGEAAEPLVMTDNDFHGKIPWGYCGNEIFNGCRSAEVHAALAERL
NALAVLLGGTSAQEQLEAAWQNVLVAQHHDITICGLLDLAHRFLPASQQAAQEADAISAS
TFASRFADPHADGVLAVNLNSFPVSAWIETPANGCSTAFDGDCAVPSELSDGMLRMLVQL
NPLEAKRLLLKQAPQQAAGSAFRWEASTGMLTTPLYRIHLTRQGIASIDSAVTGQRFVDN
GSGKLFRGYIEDVDCMNDFDSDWAVTVSAHMASAVKTGFVGSIPFRFEMCLMEGVARINC
SASFELHGERVGRTGITKGIGSDFNVNGSVHEEKLRFVLDACLSEDRRMLRDAPFSIAEW
DGQVCKPEDFWMDGAKILADTPVSPAESFQSVTYLQGLYWVALRDAAQGIAVFNRGCMGA
SVEGNELSVPLIYANEYPCGTRMLNGTFSSAFAIYPFEASISDVSVHRAALAYAYPPAAI
ALQAGFGDLTRQSFAEWTSDQESVILTALYPEDRAIYARFCNYADLEASVEFSPAFSRVT
AEVNLLGETLACCGSQLHFRPWEIKTVRITL

Enzyme Prediction     

No EC number prediction in MGYG000002061_00949.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	22	177	8.4e-20	0.5650557620817844

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10786	GH38N_AMII_like	2.11e-13	8	223	14	220	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.
cd10790	GH38N_AMII_1	8.61e-10	35	175	36	170	N-terminal catalytic domain of putative prokaryotic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). This mainly bacterial subfamily corresponds to a group of putative class II alpha-mannosidases, including various proteins assigned as alpha-mannosidases, Streptococcus pyogenes (SpGH38) encoded by ORF spy1604. Escherichia coli MngB encoded by the mngB/ybgG gene, and Thermotoga maritime TMM, and similar proteins. SpGH38 targets alpha-1,3 mannosidic linkages. SpGH38 appears to exist as an elongated dimer and display alpha-1,3 mannosidase activity. It is active on disaccharides and some aryl glycosides. SpGH38 can also effectively deglycosylate human N-glycans in vitro. MngB exhibits alpha-mannosidase activity that catalyzes the conversion of 2-O-(6-phospho-alpha-mannosyl)-D-glycerate to mannose-6-phosphate and glycerate in the pathway which enables use of mannosyl-D-glycerate as a sole carbon source. TMM is a homodimeric enzyme that hydrolyzes p-nitrophenyl-alpha-D-mannopyranoside, alpha -1,2-mannobiose, alpha -1,3-mannobiose, alpha -1,4-mannobiose, and alpha -1,6-mannobiose. The GH38 family contains retaining glycosyl hydrolases that 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. Divalent metal ions, such as zinc or cobalt ions, are suggested to be required for the catalytic activities of typical class II alpha-mannosidases. However, TMM requires the cobalt or cadmium for its activity. The cadmium ion dependency is unique to TMM. Moreover, TMM is inhibited by swainsonine but not 1-deoxymannojirimycin, which is in agreement with the features of cytosolic alpha-mannosidase.
smart00872	Alpha-mann_mid	3.76e-08	286	335	15	65	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.
pfam01074	Glyco_hydro_38	7.67e-08	21	186	22	186	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10789	GH38N_AMII_ER_cytosolic	9.28e-08	19	193	15	192	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJE29876.1	1.01e-151	8	811	30	825
AST55805.1	1.10e-150	8	811	30	825
QUT97323.1	4.32e-150	8	811	30	825
BBL06663.1	2.70e-23	2	805	53	865
VTR43839.1	1.80e-22	8	671	27	698

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
1.000061	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002061_00949.