dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: HUMAN GUT

help

CAZyme Information: MGYG000003251_01480

You are here: Home > Sequence: MGYG000003251_01480

Basic Information help

Species

Porphyromonas_A sp001808555

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae; Porphyromonas_A; Porphyromonas_A sp001808555

CAZyme ID

MGYG000003251_01480

CAZy Family

GH18

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
471	MGYG000003251_443\|CGC1	52664.94	4.8874

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003251	1810024	MAG	United States	North America

Gene Location

Start: 1420; End: 2835 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000003251_01480.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06542	GH18_EndoS-like	1.22e-31	194	437	1	242	Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.
cd11337	AmyAc_CMD_like	0.007	261	319	80	148	Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is mainly bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AMD86130.1	6.47e-125	91	471	79	462
SNV13754.1	6.47e-125	91	471	79	462
ASF43972.1	3.78e-122	1	469	1	463
AIP98746.1	1.14e-121	56	469	48	464
AFL96562.1	1.14e-121	56	469	48	464

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1EDT_A	1.56e-44	197	456	12	264	ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H, ENDO H [Streptomyces plicatus]
6VE1_A	2.04e-44	197	456	16	268	ChainA, Endo-beta-N-acetylglucosaminidase H [Streptomyces plicatus],6VE1_B Chain B, Endo-beta-N-acetylglucosaminidase H [Streptomyces plicatus],6VE1_C Chain C, Endo-beta-N-acetylglucosaminidase H [Streptomyces plicatus],6VE1_D Chain D, Endo-beta-N-acetylglucosaminidase H [Streptomyces plicatus]
1C90_A	3.61e-44	197	456	7	259	ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H [Streptomyces plicatus],1C90_B Chain B, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H [Streptomyces plicatus]
1C91_A	3.61e-44	197	456	7	259	ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H [Streptomyces plicatus]
1C8X_A	5.04e-44	197	456	7	259	ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H [Streptomyces plicatus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P04067	2.55e-43	197	456	54	306	Endo-beta-N-acetylglucosaminidase H OS=Streptomyces plicatus OX=1922 PE=1 SV=1
P80036	3.63e-34	188	461	50	313	Endo-beta-N-acetylglucosaminidase OS=Flavobacterium sp. (strain SK1022) OX=148444 PE=1 SV=2
P36911	4.29e-33	194	457	60	326	Endo-beta-N-acetylglucosaminidase F1 OS=Elizabethkingia meningoseptica OX=238 GN=endOF1 PE=1 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
0.000000	0.000000	1.000043	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000003251_01480.