CAZyme Information: MGYG000003091_01311

Basic Information

• Species: Parabacteroides sp900547435
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp900547435
• CAZyme ID: MGYG000003091_01311
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
967	MGYG000003091_61|CGC1	110204.46	5.3036

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003091	3044653	MAG	Spain	Europe

• Gene Location: Start: 5685; End: 8588 Strand: +

Full Sequence      

MNLHNLLLMGALLVSPALFAQEHSGGVPEMKADCYPAVYKSDKGMMQRVWVTIPHEGKPL
SVTLGLGEQTQRVKLNEGTNRFYFEIPEVSQSVRLPLTLKQGKTLLASQEIPVEPVRHWQ
MNLVQHTHTDIGYTRSQMEILAEHLRYIDYALDYCDATDNYPDYAKFRWTCEISWAVSEY
LKHRPKEQVERLKQRVKEGRIELATMYLNFDELPDEQTLAASLAPVKQFREEGMRAELAM
QDDVNGIGWCFSEYFADAGIKYVNMGTHGHRALICFDVPTVFWWQSPSGKKVLAYRAEHY
NQGNFFGVHTDDFETFEQRVLEYLGQLEDKGYPYDICAAQHSGYFTDNAPPSTKSSEMVM
RWNEKYEWPKLRTAVATDFIKTIEQKYADRIETIRGAWPDWWTDGFASGAREAAVSRVTH
SNVIANQAGLSFAKLLGASLPEDVNRKIDEVNDALLFYDEHTFGYSESVRDPYGLETWEQ
RSLKQSYAWEAYRHTGLLGEITMGVLQQFVPKAQVPSVAVFNALNWSYSGIARVYIDHQI
LPKEKDFEIVDASGKAIPAQVGESRSDGTYWNLYVKDVPALGYAQYYIQVKDAPRPVVQT
SDALVETHVENAWYAVDFNPSKGTISRLYDKELGKSLLTPDAEWELGEFIYEIVDSRHPM
EQYRAPQFLRRSPEKMRFDRYEQGDIYDIYRFRGETPAGREPDNLMVEYRLYKVEKKIEV
AYWLRKKAVTDPESVYISFPYQVEDGKIHLDVPGGNIEAGVDQIPGSSNDWYTVQNFATA
RNGASQVVMGSQEIPLMQFGAINTGRYKAGAVPQSTNMYSWPMNNYWVTNFNADQMGAMK
WSYFITSSGDNSLDYATKFAWSNRIPFLTRVLPADKEASASSSLQPASILNIQPSNLLLV
SMKPVEGENAVMLQLREVGGRSAKFSIVSDKVNIRRITVCDVVGDPLPGNPSPDFLPWEN
KFIKVGW

Enzyme Prediction     

No EC number prediction in MGYG000003091_01311.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	121	390	5e-19	0.9479553903345725

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	1.65e-91	120	364	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.
pfam01074	Glyco_hydro_38	4.77e-30	120	386	1	258	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10786	GH38N_AMII_like	1.73e-15	121	363	2	250	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.
PRK09819	PRK09819	3.27e-09	510	635	378	514	mannosylglycerate hydrolase.
cd10814	GH38N_AMII_SpGH38_like	3.40e-09	144	396	22	265	N-terminal catalytic domain of SPGH38, a putative alpha-mannosidase of Streptococcus pyogenes, and its prokaryotic homologs; glycoside hydrolase family 38 (GH38). The subfamily is represented by SpGH38 of Streptococcus pyogenes, which has been assigned as a putative alpha-mannosidase, and is encoded by ORF spy1604. 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. A divalent metal ion, such as a zinc ion, is required for its activity. SpGH38 is inhibited by swainsonine. The absence of any secretion signal peptide suggests that SpGH38 may be intracellular.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT95977.1	0.0	24	967	23	962
AST53023.1	0.0	24	967	23	962
BBK90267.1	0.0	24	967	23	962
ABR43377.1	0.0	24	967	23	962
QRO16434.1	0.0	24	967	23	962

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
0.000255	0.999093	0.000177	0.000160	0.000151	0.000143

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003091_01311.