CAZyme Information: MGYG000002614_00098

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola
• CAZyme ID: MGYG000002614_00098
• CAZy Family: GH95
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
798		88507.74	5.7656

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002614	2560607	MAG	China	Asia

• Gene Location: Start: 9801; End: 12197 Strand: +

Full Sequence      

MNKLYSVVLLLVLGLCSCTKEVSETTNHLKLWYVTPADATTADNPDPWTDDAAWLKALPL
GNGSLGAMVFGDVNKERIQLNEETMWSGSPQESDNPQAAAHLDKIKELLFAGKYKEATEL
TNRTQVCTGSGSGSGVGAAVPFGCFQTMGDLWIDFDNKAAYTDYYRELDLNEATARVSYV
QDGVTYRREIFVSYPAQAMVVKLTASQAAKLSFTCKMTRPEHFRTYSENNQLIMTGALSD
GKGGEGLQYMARLSAAVQNGTLSLTDSTLSVSSADEVVLYLTASTDYQLQYPTYKGRDYA
TLSANALQKAMRQSYTQLREDHLKEYQSYYNRAEFSLAQATDTVPTDISVQRAREGQVSP
HLYELMFQYGRYLLISSSRPGTLPANLQGIWANKIQTPWNGDYHTDVNVEMNYWPAEVTN
LSECHLPLFDLIASLVDPGTRTARIQYNKKGWVVHPITNVWGYTSPGEYASWGMHTGAPA
WICQHIYEHYRFTGDEKFLKDMYPVLKGAVEFYMDWLTVDPKTGKLVSGPAVSPENTFVA
PDGSHCQISMGPSHDQQTIWQLFTDFIDASHQLSVSDAFVSEVSAAREKLLGIQVGSDGR
IMEWAEEFPEVEPGHRHISHLFALHPGAQINPLQTPDLTQAASKSLDYRIEHGGGHTGWS
AAWLVSLYARLQQSDKALACLDKVLMKSLNPNLFTLCPPFQIDANFGTTAGIAEMLLQSH
VLDGDTYVIQILPSLPAEWQTGSFTGLKARGGFEVSARWKNGKLTAASVKSLLGHKCRIV
YGGSSQDLQLSKGQEWKW

Enzyme Prediction     

EC	3.2.1.63

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH95	26	786	3e-278	0.9889196675900277

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam14498	Glyco_hyd_65N_2	9.66e-84	31	287	1	231	Glycosyl hydrolase family 65, N-terminal domain. This domain represents a domain found to the N-terminus of the glycosyl hydrolase 65 family catalytic domain.
pfam04685	DUF608	0.009	486	516	108	138	Glycosyl-hydrolase family 116, catalytic region. This represents a family of archaeal, bacterial and eukaryotic glycosyl hydrolases, that belong to superfamily GH116. The primary catabolic pathway for glucosylceramide is catalysis by the lysosomal enzyme glucocerebrosidase. In higher eukaryotes, glucosylceramide is the precursor of glycosphingolipids, a complex group of ubiquitous membrane lipids. Mutations in the human protein cause motor-neurone defects in hereditary spastic paraplegia. The catalytic nucleophile, identified in UniProtKB:Q97YG8_SULSO, is a glutamine-335, with the likely acid/base at Asp-442 and the aspartates at Asp-406 and Asp-458 residues also playing a role in the catalysis of glucosides and xylosides that are beta-bound to hydrophobic groups. The family is defined as GH116, which presently includes enzymes with beta-glucosidase, EC:3.2.1.21, beta-xylosidase, EC:3.2.1.37, and glucocerebrosidase EC:3.2.1.45 activity.
pfam06202	GDE_C	0.010	478	534	85	145	Amylo-alpha-1,6-glucosidase. This family includes human glycogen branching enzyme AGL. This enzyme contains a number of distinct catalytic activities. It has been shown for the yeast homolog GDB1 that mutations in this region disrupt the enzymes Amylo-alpha-1,6-glucosidase (EC:3.2.1.33).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT74196.1	0.0	8	798	6	795
QMU26635.1	0.0	10	795	6	793
AUC23986.1	0.0	12	794	15	791
QTE23654.1	0.0	3	796	12	800
QOD61756.1	0.0	3	796	12	800

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7KMQ_A	1.74e-166	29	785	41	763	ChainA, Glyco_hyd_65N_2 domain-containing protein [Xanthomonas citri pv. citri str. 306],7KMQ_B Chain B, Glyco_hyd_65N_2 domain-containing protein [Xanthomonas citri pv. citri str. 306]
4UFC_A	1.76e-163	29	779	22	741	Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus]
2RDY_A	4.97e-157	54	780	14	753	ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125]
2EAB_A	1.74e-124	31	793	20	864	Crystalstructure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAB_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAC_A Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum],2EAC_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum]
2EAD_A	1.31e-123	31	793	20	864	ChainA, Alpha-fucosidase [Bifidobacterium bifidum],2EAD_B Chain B, Alpha-fucosidase [Bifidobacterium bifidum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8L7W8	3.32e-155	54	794	63	827	Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1
A2R797	2.52e-96	57	761	38	758	Probable alpha-fucosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=afcA PE=3 SV=1
Q5AU81	5.17e-87	60	759	46	775	Alpha-fucosidase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=afcA PE=1 SV=1
Q2USL3	1.35e-66	48	780	19	715	Probable alpha-fucosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=afcA PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000350	0.207613	0.791724	0.000100	0.000109	0.000110

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002614_00098.