dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000003250_01346

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Basic Information help

Species

UMGS1880 sp900761765

Lineage

Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-552; UMGS1880; UMGS1880 sp900761765

CAZyme ID

MGYG000003250_01346

CAZy Family

GH3

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1271		138612.31	4.0465

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003250	1644369	MAG	United States	North America

Gene Location

Start: 5013; End: 8828 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000003250_01346.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH3	731	905	2.7e-34	0.7870370370370371

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01915	Glyco_hydro_3_C	2.37e-14	131	332	2	184	Glycosyl hydrolase family 3 C-terminal domain. This domain is involved in catalysis and may be involved in binding beta-glucan. This domain is found associated with pfam00933.
PRK15098	PRK15098	5.37e-14	97	510	351	737	beta-glucosidase BglX.
pfam01391	Collagen	6.08e-12	33	68	18	53	Collagen triple helix repeat (20 copies). Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
pfam00933	Glyco_hydro_3	6.64e-12	732	901	84	255	Glycosyl hydrolase family 3 N terminal domain.
pfam01391	Collagen	3.09e-10	33	73	6	46	Collagen triple helix repeat (20 copies). Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VEU80230.1	2.00e-158	103	1092	28	1009
QOS39237.1	4.78e-144	100	1078	43	1034
VEU80232.1	4.56e-140	104	924	66	882
QEN05281.1	3.52e-126	73	922	37	883
QOL35078.1	5.52e-125	87	922	51	874

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5WUG_A	4.34e-58	126	920	44	763	Expression,characterization and crystal structure of a novel beta-glucosidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii],5WVP_A Expression, characterization and crystal structure of a novel beta-glucosidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
2X42_A	2.24e-21	690	917	3	258	Structureof beta-glucosidase 3B from Thermotoga neapolitana in complex with alpha-D-glucose [Thermotoga neapolitana DSM 4359]
2X40_A	2.24e-21	690	917	3	258	Structureof beta-glucosidase 3B from Thermotoga neapolitana in complex with glycerol [Thermotoga neapolitana DSM 4359],2X41_A Structure of beta-glucosidase 3B from Thermotoga neapolitana in complex with glucose [Thermotoga neapolitana DSM 4359]
3AC0_A	8.95e-17	692	917	7	241	Crystalstructure of Beta-glucosidase from Kluyveromyces marxianus in complex with glucose [Kluyveromyces marxianus],3AC0_B Crystal structure of Beta-glucosidase from Kluyveromyces marxianus in complex with glucose [Kluyveromyces marxianus],3AC0_C Crystal structure of Beta-glucosidase from Kluyveromyces marxianus in complex with glucose [Kluyveromyces marxianus],3AC0_D Crystal structure of Beta-glucosidase from Kluyveromyces marxianus in complex with glucose [Kluyveromyces marxianus]
5NBS_A	2.70e-16	121	429	387	656	Structuralstudies of a Glycoside Hydrolase Family 3 beta-glucosidase from the Model Fungus Neurospora crassa [Neurospora crassa OR74A],5NBS_B Structural studies of a Glycoside Hydrolase Family 3 beta-glucosidase from the Model Fungus Neurospora crassa [Neurospora crassa OR74A]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P15885	3.78e-54	122	903	13	699	Beta-glucosidase OS=Ruminococcus albus OX=1264 PE=3 SV=1
P16084	4.32e-53	113	902	20	771	Beta-glucosidase A OS=Butyrivibrio fibrisolvens OX=831 GN=bglA PE=3 SV=1
A1CA51	1.96e-20	692	992	7	310	Probable beta-glucosidase I OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=bglI PE=3 SV=1
P27034	7.52e-20	692	917	3	238	Beta-glucosidase OS=Rhizobium radiobacter OX=358 GN=cbg-1 PE=3 SV=1
Q2U8Y5	7.73e-20	692	917	7	241	Probable beta-glucosidase I OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=bglI PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.002864	0.047680	0.949196	0.000069	0.000093	0.000073

TMHMM Annotations download full data without filtering help

start	end
12	34