CAZyme Information: MGYG000003835_00597

Basic Information

• Species: UBA7173 sp001915385
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173; UBA7173 sp001915385
• CAZyme ID: MGYG000003835_00597
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
969		107564.05	5.3269

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003835	3225656	MAG	United States	North America

• Gene Location: Start: 14659; End: 17568 Strand: -

Full Sequence      

MNNIRTVVATMCMVCAVTQLPAEVTPQTVQYEVKPMYGFRKDKAPGRIVNVKLQGGELSG
KFTVEAKCGTKKEKKSYNITGEGESTVEFLLPKSVGVDKDETVVMTLRADGKEFRDTIAV
PQMRQFTVYLFNHSHVDIGYTNTHKNIETLHKNNVIEGMRLGHETENYPDGAQMVWNPEV
TWPIERLWNSQPELRDSIISAIKLGHIAVDASYVNLNTSICADEELFHLFGFSRKMQELS
GKDADVFAQFDIPGISWGLVPVLANQGIKYVMSWTNGGDRIGHAREGLDGKPFWWVGPDG
KSKVLFFQPGNYANSGSMGKGGETGRPWLGQRNAAKVPRFIKMGYANVDFTKQLTELQNS
DYPYDFACFSWTLWDNNPIDADIPDAVKEWNEKYAYPHIKISSAHEIMKMVDERYGDKLP
VVSGDYTEYWTDGLGTAAVLTAANRHSKERMIQVETVASLLADQGVPAPRADIEEAWRHI
ILGSEHTWCFENPNDAYFSDAILNVKKSYFEDAEKRSLALLDEVLAPVTDKANGAFGPYD
GPAEGGVTVINTHSWPHGGIVTLPYKESMRGNRVVDDSGNEVLCQRLASGELVFLANETP
AFGTTHYTVVSGDCSVPTSNSVSKSEISNGVVKVNIDTVTGNITSLRINGSDYNYINKGA
NQFVWLPANVDEPQTDKVVSIEITENGPLVSEVTVTSEARGCNSLTRSVRLIAGQPWVEI
SNTVDKQATPDKESIHFGFDFNVPQAVTNIDIPWGVMQPEKDQWKQANRNWMALQRWADI
SNDTHGVTWCSLDAPLMEYGGRSANIATGWGNGGDWKYSLPEHSAEIYSWAMNNHWHTNF
PQTQEGKVTFSYRMMPHGTSDLAAANRFGMEQAQPLVHVIAKNATELKAPVAIDNSNVVV
SIVKDQGDGKSFIVRLRSLSDKEENVTMTYPRRTPASVHICDLGEEPSRPADGTLTLPPY
GMTTLLLKW

Enzyme Prediction     

No EC number prediction in MGYG000003835_00597.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	1.14e-68	127	392	1	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	2.71e-16	627	788	1	174	Glycosyl hydrolases family 38 C-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
COG0383	AMS1	1.03e-10	436	967	456	941	Alpha-mannosidase [Carbohydrate transport and metabolism].
pfam01074	Glyco_hydro_38	1.20e-09	127	429	1	270	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10786	GH38N_AMII_like	3.81e-07	127	300	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AOW10592.1	0.0	18	969	22	968
AOW10591.1	0.0	14	969	18	970
AUN37913.1	0.0	18	969	22	968
SDS34905.1	0.0	33	968	54	990
AUN37912.1	5.83e-285	272	969	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
0.000774	0.954614	0.043652	0.000345	0.000308	0.000276

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003835_00597.