CAZyme Information: MGYG000001334_01457

Basic Information

• Species: Ligilactobacillus ruminis
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Ligilactobacillus; Ligilactobacillus ruminis
• CAZyme ID: MGYG000001334_01457
• CAZy Family: CBM34
• CAZyme Description: Intracellular maltogenic amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
587	MGYG000001334_2|CGC5	68619.12	4.7147

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001334	2103640	Isolate	not provided	not provided

• Gene Location: Start: 422391; End: 424154 Strand: -

Full Sequence      

MEISALYHRPDSEMAYLKTKDAFQIRLRTKHSDVKEVKLLYGDPYGNKVNEKDESTWEHD
VISMEKTFETKYHDYWETEVKMPLNRLQYAFHLVGNDGEEILYDDRRVMPYTEENEGKLS
CFRMPYLHEIDRVKTPEWVRKTVWYQIFPERFANGDKTNDPNGTLPWGSADPTPTNFFGG
DLKGILDHLDYLQDLGVNGLYLCPIFTATSNHKYDTVDYFGIDPAFGDKETLKELVDAAH
ERGMHVMLDAVFNHMGDFSMQWKDVQKYGENSRFAKWFHINKFPVSYDETGNAEHAENLT
YEVFSTTPHMPKLNTANEETAEYLLEIAQYWIKEFDIDAWRLDVANEIDHHFWKRFYAAT
HELKSDFYILGEVWHSAQEWAEQEEFDAVMNYPFTESIALDFVNHETTAKEMVSMLSEHL
MKYRDQTNEVMLNAMDTHDTARLLTLCHGNKELQRQTLAFMFTQPGAPCVYYGTEVGLDG
GFDPGCRKCMIWDEEKQDHEMFAFMQKLIKLRKDYADIWSKGKVEYRNVCDETNSLEVVR
SFDGVELHCFFNMGEKALEAPCSGEVLLGQNLKDDKVEKDGFIIVRK

Enzyme Prediction     

EC	3.2.1.54	3.2.1.133	3.2.1.135

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	180	484	2.7e-126	0.9966666666666667
CBM34	7	131	4.9e-31	0.975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	0.0	142	520	2	386	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	3.74e-106	6	515	5	523	maltodextrin glucosidase; Provisional
pfam00128	Alpha-amylase	6.06e-79	180	484	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.
cd11353	AmyAc_euk_bac_CMD_like	4.52e-77	142	513	2	356	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.
COG0366	AmyA	1.36e-74	142	570	1	500	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEN79099.1	0.0	1	587	1	587
SFV39857.1	2.56e-307	1	586	1	589
QCQ04931.1	5.46e-291	1	584	1	583
QIA89092.1	2.10e-288	1	584	1	583
AWZ39825.1	6.00e-288	1	584	1	583

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7D9B_A	1.79e-196	3	584	4	583	ChainA, Alpha-glycosidase [Weissella cibaria]
7D9C_A	5.09e-196	3	584	4	583	ChainA, Alpha-glycosidase [Weissella confusa],7DCG_A Chain A, Alpha-glycosidase [Weissella cibaria],7DCH_A Chain A, Alpha-glycosidase [Weissella cibaria]
7EHH_A	1.02e-195	3	584	4	583	ChainA, alpha-glucosidase [Weissella cibaria],7EHI_A Chain A, alpha glucosidase [Weissella cibaria]
1J0H_A	5.81e-187	1	546	1	529	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	1.65e-186	1	546	1	529	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	5.10e-198	1	554	1	538	Intracellular maltogenic amylase OS=Bacillus subtilis OX=1423 GN=bbmA PE=1 SV=2
O06988	2.05e-197	1	554	1	538	Intracellular maltogenic amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=bbmA PE=3 SV=2
P38940	6.38e-186	1	546	1	529	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
A0A7U9P668	2.37e-183	1	561	1	545	Cyclomaltodextrinase OS=Geobacillus thermopakistaniensis (strain MAS1) OX=1408282 GN=T260_08735 PE=1 SV=1
P32818	1.02e-173	5	585	5	584	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
1.000054	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001334_01457.