CAZyme Information: MGYG000001528_00712

Basic Information

• Species: Mediterraneibacter massiliensis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter massiliensis
• CAZyme ID: MGYG000001528_00712
• CAZy Family: GH13
• CAZyme Description: Cyclomaltodextrinase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
437		50594.22	5.3987

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001528	3068303	Isolate	not provided	not provided

• Gene Location: Start: 577275; End: 578588 Strand: -

Full Sequence      

MWAYNETFYQIYPIGFCGAPAHNDGLCVPRIQKIGDWSEYLEQLGIGSIILNPVFESDNH
GYDTRDFKKIDCRLGTNDDFKKICKILHEHHIKIILDGVFNHVGRGFWAFSDVQEKKWDS
PYKDWFYINFDGNSGYDDGFWYEGWEGHFELVKLNLQNPEVKNYLLDCVKFWIQEFDIDG
LRLDVAYSLDHDFMKSLRRYCEEIKPGFALIGEVLFGDYNIIVNDEMLHSCTNYECYKGI
YSSFNCMNLFEIAHSLNRQYGKEPWCLYRGKHLMNFVDNHDVTRIASILTNKKHLPLAYG
LLFGMPGIPCIYYGSEWGEEGEKAPGSDHALRPCFSAPNANELTDFIRTLIHIRKNSPAL
CSGGYENILITNHQLIFERRTENERLLVAINASEHPYTAYDNRVSGNYHELITGAAGTLE
GQCLLPPYSVRYYDFCC

Enzyme Prediction     

EC	3.2.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	33	325	2.6e-80	0.9833333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11353	AmyAc_euk_bac_CMD_like	0.0	5	365	1	366	Alpha amylase catalytic domain found in eukaryotic and bacterial 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.
cd11337	AmyAc_CMD_like	0.0	8	365	2	328	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.
cd11338	AmyAc_CMD	5.03e-106	31	365	59	389	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). 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.
cd11354	AmyAc_bac_CMD_like	2.43e-91	8	360	4	352	Alpha amylase catalytic domain found in bacterial 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 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.
PRK10785	PRK10785	7.82e-59	2	394	118	560	maltodextrin glucosidase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL25290.1	8.06e-272	1	432	1	436
QEK16270.1	1.97e-269	1	433	1	433
QEI31832.1	9.31e-269	1	432	1	436
QRT30571.1	9.31e-269	1	432	1	436
QHB24324.1	9.31e-269	1	432	1	436

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7D9B_A	1.02e-55	2	390	139	549	ChainA, Alpha-glycosidase [Weissella cibaria]
1EA9_C	2.49e-55	2	398	127	540	Cyclomaltodextrinase[Bacillus sp. (in: Bacteria)],1EA9_D Cyclomaltodextrinase [Bacillus sp. (in: Bacteria)]
7D9C_A	2.75e-55	2	390	139	549	ChainA, Alpha-glycosidase [Weissella confusa],7DCG_A Chain A, Alpha-glycosidase [Weissella cibaria],7DCH_A Chain A, Alpha-glycosidase [Weissella cibaria]
7EHH_A	5.32e-55	2	390	139	549	ChainA, alpha-glucosidase [Weissella cibaria],7EHI_A Chain A, alpha glucosidase [Weissella cibaria]
1SMA_A	7.27e-54	2	433	131	583	CrystalStructure Of A Maltogenic Amylase [Thermus sp. IM6501],1SMA_B Crystal Structure Of A Maltogenic Amylase [Thermus sp. IM6501]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q08341	2.08e-58	2	396	130	540	Cyclomaltodextrinase OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1
P32818	5.28e-56	2	420	131	575	Maltogenic alpha-amylase OS=Bacillus acidopullulyticus OX=28030 PE=3 SV=1
Q59226	8.77e-55	2	398	127	540	Cyclomaltodextrinase OS=Bacillus sp. OX=1409 GN=CDI5 PE=1 SV=1
Q9R9H8	5.53e-54	2	388	133	532	Intracellular maltogenic amylase OS=Bacillus subtilis OX=1423 GN=bbmA PE=1 SV=2
A0A7U9P668	1.48e-53	2	433	131	583	Cyclomaltodextrinase OS=Geobacillus thermopakistaniensis (strain MAS1) OX=1408282 GN=T260_08735 PE=1 SV=1

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
1.000069	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001528_00712.