CAZyme Information: MGYG000002313_01042

Basic Information

• Species: Lactobacillus mulieris
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lactobacillus; Lactobacillus mulieris
• CAZyme ID: MGYG000002313_01042
• CAZy Family: CBM34
• CAZyme Description: Intracellular maltogenic amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
568		66219.74	5.8965

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002313	1675234	Isolate	Japan	Asia

• Gene Location: Start: 300; End: 2006 Strand: +

Full Sequence      

MQEASLRHRPESEDCFVIDKTHLRLRFHTAKDDVKKVIVHYLDSYYDLKTAQTKEMEKIG
SGQVAEYYMTTLELPLHRCQYTFEVVGEDGSHLIYGDRGIREFNDSNLYDYGQFFKVPYF
HEIDMAKTPAWVKETVWYQIFPERFNNGDKSNDPVGTKPWNPSDHPGREDYYGGDLQGVL
DKLDYLQSLGINGLYFCPIFKASSNHKYDTIDYLEIDPDFGDKTLFKKLVDEAHKRGMHV
MLDAVFNHLGDQSRQWQDVVQNGRNSKYFNWFHINRLPVMPFTDPTKGEQLPPYDTFAFE
KHMPKLNTANEDVQKYLLNIATYWVKEFHIDAWRLDVANEVDHHFWKKFHVELMNINPEF
YIVGEVWHSSQPWLNGDEFTGVMNYPYTQQIEDHFLTKKISAKMLTEVLFDQLMLYRDCV
NSGMLNMLDSHDTARLLTLAGDNKDRALCALAFELVQPGSPSIYYGTEMAMTGGNDPDCR
KPMDWTKEGDSYWQKVHDLIKFRRKHSTVLSRSDIKFAIKDELIVIKHGEITAYFNTSNH
EVEITKKCSVSNGYQNGVLSPNGYILCE

Enzyme Prediction     

EC	3.2.1.1	3.2.1.41

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	174	477	1.5e-127	0.9966666666666667
CBM34	7	125	4.8e-29	0.9833333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	0.0	134	515	1	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.
PRK10785	PRK10785	3.38e-92	55	517	50	533	maltodextrin glucosidase; Provisional
pfam00128	Alpha-amylase	4.93e-80	174	477	1	334	Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.
COG0366	AmyA	4.64e-73	135	559	1	505	Glycosidase [Carbohydrate transport and metabolism].
cd11316	AmyAc_bac2_AmyA	5.70e-67	136	492	2	355	Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Chloroflexi, Dictyoglomi, and Fusobacteria. 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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGR96187.1	0.0	1	568	1	568
APT14093.1	0.0	1	568	1	568
ASY54335.1	1.86e-300	1	566	1	570
QTH65636.1	1.52e-299	1	566	1	570
QTD65940.1	1.52e-299	1	566	1	570

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7D9B_A	1.47e-195	4	566	5	583	ChainA, Alpha-glycosidase [Weissella cibaria]
7D9C_A	4.19e-195	4	566	5	583	ChainA, Alpha-glycosidase [Weissella confusa],7DCG_A Chain A, Alpha-glycosidase [Weissella cibaria],7DCH_A Chain A, Alpha-glycosidase [Weissella cibaria]
7EHH_A	8.40e-195	4	566	5	583	ChainA, alpha-glucosidase [Weissella cibaria],7EHI_A Chain A, alpha glucosidase [Weissella cibaria]
1J0H_A	5.50e-161	1	522	1	515	Crystalstructure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0H_B Crystal structure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0I_A Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus],1J0I_B Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus]
1J0J_A	1.56e-160	1	522	1	515	ChainA, neopullulanase [Geobacillus stearothermophilus],1J0J_B Chain B, neopullulanase [Geobacillus stearothermophilus],1J0K_A Chain A, neopullulanase [Geobacillus stearothermophilus],1J0K_B Chain B, neopullulanase [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9R9H8	2.47e-167	1	522	1	515	Intracellular maltogenic amylase OS=Bacillus subtilis OX=1423 GN=bbmA PE=1 SV=2
O06988	9.89e-167	1	522	1	515	Intracellular maltogenic amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=bbmA PE=3 SV=2
P38940	1.71e-159	1	522	1	515	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
A0A7U9P668	1.24e-156	1	544	1	544	Cyclomaltodextrinase OS=Geobacillus thermopakistaniensis (strain MAS1) OX=1408282 GN=T260_08735 PE=1 SV=1
P32818	3.31e-156	1	517	1	511	Maltogenic alpha-amylase OS=Bacillus acidopullulyticus OX=28030 PE=3 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
1.000028	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002313_01042.