CAZyme Information: MGYG000001372_01447

Basic Information

• Species: Paraprevotella xylaniphila
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Paraprevotella; Paraprevotella xylaniphila
• CAZyme ID: MGYG000001372_01447
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
969		107551.36	5.7907

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001372	3789432	Isolate	not provided	not provided

• Gene Location: Start: 56303; End: 59212 Strand: -

Full Sequence      

MKRNFFCGMLAVLAAGNVNADVVPEQVSCVVKPLYGYRQDRSPGRIVAVRLKGAELKGEV
CVDVAYRKLKETSAFRIDAEDSAEVEVMLPSALPVDKTVDVSLTVRGTEKKVKTKVTVEP
MRHWTVYLYNHSHVDIGYTNTHKNVEMLHKTNVKEGMKLSHETVGHVDGARFVWNPEVTW
PIERLWNSEPGMRDEIIASIKGGGLSVDASYLNLNTSICSDEELFHVFKFSRELQRLSGV
PADVFQQFDIPGISWGLVPVMAQEGIKYVISWPNTDRGGNAHSFGIDGFPFWWVGPDGHS
KVLFLQPGKYANSGSMDKGNTTGRPWFGQRNARKVPARIQMGSANVDFTGQLVDLEKKNY
PYDFIVLSWSLWDNNPVDADVPYAVNEWNKKYAYPKIVISGGHEVMKTLEEKYGDRLPVV
HGDYTEYWTDGLGTAARLTAVNRRNKERITQAETVWSMLAGGACAPRAEFDEGWRYILLG
SEHTWDFENPWEPYFHEAISKVKQSYFYEAEARSMTLLDEALGLATDKSNGALGPREGPS
NGGIAVFNTLSWPHGGLVTLSSSESQKGDKVVDDVGNAVPSQRLSTGELAFWASDVPALG
SRHYRVVEGDAVPGDACKLDGYTLDNGCVRVTIDGKTGNIVSLTRAGEDYNYIDASVDGG
ANSCSWLPANENKPEADKVQAITVTEQGGLVVELKVQSMMKGCRSVTRTVRLVAGQPWVE
TTNVVDKLPLLDKDGIHFGFGFNVPQGVTKVDIPWGIMEVEKDQWPQANRNWMALQRWLD
VSNDTHGVTWCALDAPLFEYGDRTANISLGWGGQGPWLTKLEPSSTVYSWAMNNHWHTNF
PLTQDGPVAFRYRIHPHGGYDAVDANRFGLEQAQPLVHVTADKNPDVKSVISVDNRAVYV
TVLKSTEKDNEMIVRLRSVSDREETVALDFPAHRPSSVSLCTLEEQPGQIVDGTLTMKPY
GMATLKLTF

Enzyme Prediction     

No EC number prediction in MGYG000001372_01447.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	1.56e-74	125	390	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	6.84e-11	624	789	1	174	Glycosyl hydrolases family 38 C-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
COG0383	AMS1	9.93e-10	402	969	420	943	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10786	GH38N_AMII_like	2.34e-07	125	298	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	2.48e-04	125	427	1	270	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AOW10591.1	0.0	9	969	15	970
AOW10592.1	0.0	9	969	15	968
SDS34905.1	0.0	6	967	19	989
AUN37913.1	0.0	1	969	7	968
AUN37912.1	0.0	270	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
0.000299	0.999012	0.000191	0.000164	0.000154	0.000144

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001372_01447.