CAZyme Information: MGYG000004265_01963

Basic Information

• Species: UMGS263 sp900540535
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS263; UMGS263 sp900540535
• CAZyme ID: MGYG000004265_01963
• CAZy Family: GH116
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
316		36388.41	8.1876

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004265	2478899	MAG	China	Asia

• Gene Location: Start: 79513; End: 80463 Strand: +

Full Sequence      

MCTLAGHIKLKPGENGSIRFVLTWYFPVFEKYWGGFKFKRPSWKNYYASLFSGSDETAEY
CLKNFDSLFEKTKLFTDALYSTTIPEKALEAAGANLAVLKSTTCMRLEDGTFYAFEGTNA
DTGSCEGSCTHVWNYAYALPFLFPFLERSMRDSDYKYNSTKTGEMKFRLMLPIGSKPWNF
RACVDGQFGGIIKLYRDWKISGDDEFLKRNWKEAKKALEYAWSDKNPDKWDPEKSGVITG
RQHHTLDVELFGANPWLTGFYIGGLIAGAEIADYLGEKDSADEYRRIAEKGKKYIDKELW
NGRYYIQKIDVKIKIH

Enzyme Prediction     

No EC number prediction in MGYG000004265_01963.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH116	110	310	4.9e-31	0.6060606060606061

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam04685	DUF608	2.37e-25	125	305	6	216	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.
COG4354	COG4354	4.16e-21	13	306	254	571	Uncharacterized protein, contains GBA2_N and DUF608 domains [Function unknown].
pfam12215	Glyco_hydr_116N	6.29e-12	1	68	244	309	beta-glucosidase 2, glycosyl-hydrolase family 116 N-term. This domain is found in bacteria, archaea and eukaryotes. This domain is typically between 320 to 354 amino acids in length. This domain is found associated with pfam04685. It is found just after the extreme N-terminus. The N-terminal is thought to be the luminal domain while the C terminal is the cytosolic domain. The catalytic domain of GBA-2 is unknown. 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 in the downstream family pfam04685.
PRK10137	PRK10137	0.009	269	313	592	635	alpha-glucosidase; Provisional
TIGR01577	oligosac_amyl	0.010	198	300	366	458	oligosaccharide amylase. The name of this type of amylase is based on the characterization of an glucoamylase family enzyme from Thermoactinomyces vulgaris. The T. vulgaris enzyme was expressed in E. coli and, like other glucoamylases, it releases beta-D-glucose from starch. However, unlike previously characterized glucoamylases, this T. vulgaris amylase hydrolyzes maltooligosaccharides (maltotetraose, maltose) more efficiently than starch (1), indicating this enzyme belongs to a class of glucoamylase-type enzymes with oligosaccharide-metabolizing activity.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUH30377.1	1.41e-135	1	314	264	584
AEE95836.1	7.69e-132	1	314	270	592
QGQ98288.1	1.25e-128	1	311	272	582
BBH18759.1	2.55e-126	3	311	275	583
QHT59778.1	5.18e-125	3	315	274	586

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5BVU_A	1.33e-08	4	305	305	637	Crystalstructure of Thermoanaerobacterium xylolyticum GH116 beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],5BX2_A Crystal structure of Thermoanaerobacterium xylanolyticum GH116 beta-glucosidase with 2-deoxy-2-fluoroglucoside [Thermoanaerobacterium xylanolyticum LX-11],5BX3_A Crystal structure of Thermoanaerobacterium xylanolyticum GH116 beta-glucosidase with deoxynojirimycin [Thermoanaerobacterium xylanolyticum LX-11],5BX4_A Crystal structure of Thermoanaerobacterium xylanolyticum GH116 beta-glucosidase with Glucoimidazole [Thermoanaerobacterium xylanolyticum LX-11],5BX5_A Crystal structure of Thermoanaerobacterium xylanolyticum GH116 beta-glucosidase with glucose [Thermoanaerobacterium xylanolyticum LX-11],5NCX_A Crystal structure of Thermoanaerobacterium xylolyticum GH116 beta-glucosidase with an covalent inhibitor [Thermoanaerobacterium xylanolyticum LX-11],5OST_A Beta-glucosidase from Thermoanaerobacterium xylolyticum GH116 in complex with Gluco-1H-imidazole [Thermoanaerobacterium xylanolyticum LX-11]
5FJS_A	1.33e-08	4	305	301	633	Bacterialbeta-glucosidase reveals the structural and functional basis of genetic defects in human glucocerebrosidase 2 (GBA2) [Thermoanaerobacterium xylanolyticum LX-11],5FJS_B Bacterial beta-glucosidase reveals the structural and functional basis of genetic defects in human glucocerebrosidase 2 (GBA2) [Thermoanaerobacterium xylanolyticum LX-11],5O0S_A Crystal structure of txGH116 (beta-glucosidase from Thermoanaerobacterium xylolyticum) in complex with unreacted beta Cyclophellitol Cyclosulfate probe ME711 [Thermoanaerobacterium xylanolyticum LX-11]
5NPF_A	1.33e-08	4	305	304	636	Crystalstructure of txGH116 (beta-glucosidase from Thermoanaerobacterium xylolyticum) in complex with beta Cyclophellitol Cyclosulfate probe ME594 [Thermoanaerobacterium xylanolyticum]
7DKS_A	1.33e-08	4	305	305	637	ChainA, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKT_A Chain A, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKU_A Chain A, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKV_A Chain A, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11]
7DKW_A	1.33e-08	4	305	305	637	ChainA, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKW_B Chain B, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKX_A Chain A, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11],7DKY_A Chain A, beta-glucosidase [Thermoanaerobacterium xylanolyticum LX-11]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9HCG7	1.79e-07	191	305	625	736	Non-lysosomal glucosylceramidase OS=Homo sapiens OX=9606 GN=GBA2 PE=1 SV=2
Q5M868	5.60e-07	191	305	616	727	Non-lysosomal glucosylceramidase OS=Rattus norvegicus OX=10116 GN=Gba2 PE=2 SV=2
Q69ZF3	2.34e-06	191	305	616	727	Non-lysosomal glucosylceramidase OS=Mus musculus OX=10090 GN=Gba2 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000051	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004265_01963.