CAZyme Information: MGYG000003277_02995

Basic Information

• Species: Duncaniella sp900762315
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Duncaniella; Duncaniella sp900762315
• CAZyme ID: MGYG000003277_02995
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
967		107087.59	5.3669

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003277	3767547	MAG	United States	North America

• Gene Location: Start: 25115; End: 28018 Strand: -

Full Sequence      

MNKKLTTALLSTVFPAMSMVAAVPSHVNCEVRPMYGYLPDGGAGRIVKVAVSGQDLDPKI
DVETVYKKARLKTTHNIAAGDTVATFEVMLPAAVPTDRKSTATVIVAGKKYKVDVDPMRH
WTVYIYNHAHVDIGYTNTHKNIEILHKSNVVEGMALGNETSGYPEGSRFVWNPEVTWPIE
RLLHSDPSREQEVVDALKKGSLAADASYVNLNTSICADEEMFHIFDYSRKLQKMSGVPAD
VFQQFDIPGVSWGLVPVMAQQGVKYVVSWPNTDRGGNDHSFGIDGMPFWWVGPDGVSKVL
FLQPGRYANSGSMDKGWTTGRPWFGQRDARKVPARIEQGDANVDFTPHLTELESQKYPYD
LIVLSWTLWDNCPLDADVPHAVKRWNDRYAYPHIIISGGHEFMSEIEKRYGDKLPVVTGD
YTEYWTDGLGSAAQFTAMNRRNKERIIQAETAWSMLSDGAAAPRDEMNEGWRNVMMGSEH
TWDFENPWEPYFHDALWKSKQAYFHEAETRSEDLLDEALGHAADKSNGALGPGEGPSNGG
ITVYNTQSWPHVGLVTLTAKESRKGDKVVGDDGVAVPSQRLSTGELVFMADAVPALGSRH
YRVVEGGSEAPATPSIIDGNSISNGIVTVSISPENGNIVSLTREGDSYNYIDTAVDGGAN
SCSWLPANVDAPVADSVLTVSVTERGPLVNEITVTSAMKGCRGVTRRVRLVAGMPWVEMT
NTVDKLPLLEKDGIHFGFGFNIPDSRTMIDIPWGVMEVEKDQWAQANRHWMAMQRWVDVS
NDIHGVAWCSLDAPLMEYGGRTANFSQGWGPQGPWKTKLDPSSTVYSWVMNNHWHTNFPL
SQDGPVDFRYRLMPHGAKSLAEVNRFGLEQAQPLLHVTSDRHNEVIPPVAVDNENVYITI
VKSTDRDNEMIVRLRSLSPSNEQVNLTFPQRAPSAVNLCTLEEIPSEPVDGALTMNPYGM
ATVKVKF

Enzyme Prediction     

No EC number prediction in MGYG000003277_02995.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	8.73e-66	122	386	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.
pfam07748	Glyco_hydro_38C	5.34e-12	622	787	1	174	Glycosyl hydrolases family 38 C-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10786	GH38N_AMII_like	2.15e-05	122	295	1	167	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.
pfam01074	Glyco_hydro_38	6.87e-05	122	424	1	270	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
pfam09261	Alpha-mann_mid	9.22e-05	423	521	1	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
AOW10592.1	0.0	6	967	21	968
AOW10591.1	0.0	6	967	21	970
AUN37913.1	0.0	13	967	18	968
SDS34905.1	0.0	24	966	47	990
AUN37912.1	8.81e-312	267	967	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
0.000302	0.998947	0.000196	0.000183	0.000171	0.000164

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003277_02995.