dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000111_02272

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Basic Information help

Species

Cutibacterium acnes

Lineage

Bacteria; Actinobacteriota; Actinomycetia; Propionibacteriales; Propionibacteriaceae; Cutibacterium; Cutibacterium acnes

CAZyme ID

MGYG000000111_02272

CAZy Family

GH33

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
502	MGYG000000111_5\|CGC2	53229.65	9.1386

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000111	2484103	Isolate	Canada	North America

Gene Location

Start: 155644; End: 157152 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000000111_02272.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH33	114	442	2.2e-81	0.9210526315789473

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd15482	Sialidase_non-viral	1.06e-87	107	449	1	339	Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
COG4409	NanH	2.94e-34	58	410	220	606	Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
pfam13088	BNR_2	6.76e-14	131	436	1	280	BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
cd18622	GH32_Inu-like	0.005	225	307	37	120	glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2). This subfamily of glycosyl hydrolase family GH32 includes endo-inulinase (inu2, EC 3.2.1.7), exo-inulinase (Inu1, EC 3.2.1.80), invertase (EC 3.2.1.26), and levan fructotransferase (LftA, EC 4.2.2.16), among others. These enzymes cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits help

Hit ID	Query Start	Query End	Hit Start	Hit End
ALT35678.1	1	502	1	502
AXM07790.1	1	502	1	502
AER04689.1	1	502	1	502
ALD70051.1	1	502	1	502
ALU23799.1	1	502	1	502

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LBU_A	0.0	31	481	5	455	ChainA, Exo-alpha-sialidase [Cutibacterium acnes],7LBV_A Chain A, Exo-alpha-sialidase [Cutibacterium acnes]
1EUR_A	8.79e-134	108	457	13	363	Sialidase[Micromonospora viridifaciens],1EUS_A Sialidase Complexed With 2-Deoxy-2,3-Dehydro-N- Acetylneuraminic Acid [Micromonospora viridifaciens]
1EUT_A	1.89e-130	108	457	13	363	Sialidase,Large 68kd Form, Complexed With Galactose [Micromonospora viridifaciens],1EUU_A Sialidase Or Neuraminidase, Large 68kd Form [Micromonospora viridifaciens]
1WCQ_A	6.70e-130	108	457	9	359	Mutagenesisof the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine. [Micromonospora viridifaciens],1WCQ_B Mutagenesis of the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine. [Micromonospora viridifaciens],1WCQ_C Mutagenesis of the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine. [Micromonospora viridifaciens]
2BZD_A	1.34e-129	108	457	9	359	Galactoserecognition by the carbohydrate-binding module of a bacterial sialidase. [Micromonospora viridifaciens],2BZD_B Galactose recognition by the carbohydrate-binding module of a bacterial sialidase. [Micromonospora viridifaciens],2BZD_C Galactose recognition by the carbohydrate-binding module of a bacterial sialidase. [Micromonospora viridifaciens]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q02834	3.54e-129	108	457	55	405	Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1
P29767	3.87e-19	105	444	371	814	Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1
P62575	8.04e-16	228	440	538	769	Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1
P62576	8.04e-16	228	440	538	769	Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1
P15698	2.76e-12	119	448	53	390	Sialidase OS=Paeniclostridium sordellii OX=1505 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000330	0.998949	0.000186	0.000214	0.000176	0.000149

TMHMM Annotations download full data without filtering help

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