CAZyme Information: MGYG000002963_03135

Basic Information

• Species: Anaerosporobacter mobilis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Anaerosporobacter; Anaerosporobacter mobilis
• CAZyme ID: MGYG000002963_03135
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
891	MGYG000002963_24|CGC2	97476.6	5.4198

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002963	5077023	MAG	United States	North America

• Gene Location: Start: 52925; End: 55600 Strand: +

Full Sequence      

MFLTKLRKQKSIFKRLVVLLLIVTLSITSINYKMIFADSNPDSTDLTTDLSEPLARALAS
TSSLSVAPTENIGDGAILQAFCWSFNTIKANMKNIADAGYTSIQTSPINAVDDSYPTMKL
YGGSDDGKGGCWWWHYQPTDWTIGNYQLGNRDEFKSMCAEADKYGIKIIVDVVPNHTANN
QSKVSSNLRNSAGGNLYHDTGFIKCNSYSDRFQCTRYSMDGGLPDVDTENRGFQNYFIKF
LNDCIASGADGFRYDTAKHIGLSDDNRPNGVTNNFWSRVTTEITNASNIFNYGEVLQGDN
ERLAAYAGEIGSTTTSSYGSKIRNAIKSNNLNKSSIQSYEVPSGMDTSDLVTWVESHDNY
INDGTWSQLDDEQIKLAWSVITARKDGAPLFFSRPYGGGPSNKWGANQIGIAGSDLYKDD
EVAAVNKFRNAMVGQGEYLENPNGDSNVLMIQRGTVGAVIVNSKYNDYSINCSTQLQDGT
YYSLTDDHNKFEVKNHIITGTIPRRGSAVLMSYTNPTTPSVSLDNFKSTFSTDSVTFTLK
AQNTTSATYKINSNNTVNYNNGDSLVIGAGDSINTEYTITLTGVDSDGKIVTQTYTTKKV
AQPLGTTVYFEKPSSWSDSIYAYIYDESGANVQIVKAWPGTAMQKESSGLYSITFTESYS
KPLVIFNDTVNQSPGTKLQGFAVENNATYDINGKKQTTTNAITIFYKTTWSTSNIHYKIG
SGAWTTVPGIAMSPSKVNGYQTITIDLGTSNSLTACFNNGNNIWDNNSTKNYTFSSSGTY
TVSDGNVTNGEPTAIPTNTITVYYYTSWSSPNIHYQIGSGSWTNVPGVRMSSSSVSGYKV
ITIDLGTNTTLTCCFNDGNNNWDNNSGKNYYLASTGTYSIKNGTITKGTPQ

Enzyme Prediction     

EC	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	83	363	5e-98	0.9887218045112782
CBM25	798	872	2.4e-27	0.9743589743589743
CBM26	607	677	1.3e-17	0.92

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	1.16e-152	74	439	1	352	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 Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. 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.
cd11317	AmyAc_bac_euk_AmyA	9.19e-29	75	359	2	238	Alpha amylase catalytic domain found in bacterial and eukaryotic 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 AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. 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.
cd11319	AmyAc_euk_AmyA	2.89e-20	84	435	41	375	Alpha amylase catalytic domain found in eukaryotic 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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.
cd11320	AmyAc_AmyMalt_CGTase_like	2.62e-17	88	358	49	313	Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins. Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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	2.90e-16	73	309	14	260	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBF43367.1	7.21e-227	70	693	61	598
BAK28504.1	2.39e-144	67	733	39	690
CBZ48832.1	2.39e-144	67	733	39	690
CBI14123.1	2.39e-144	67	733	39	690
QWX86276.1	1.31e-143	67	733	39	690

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DC0_A	5.36e-110	71	510	2	419	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1BAG_A	5.79e-105	71	510	5	422	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
1UA7_A	1.45e-104	71	510	2	419	ChainA, Alpha-amylase [Bacillus subtilis]
2LAA_A	1.96e-24	798	890	5	102	SolutionStrucuture of the CBM25-1 of beta/alpha-amylase from Paenibacillus polymyxa [Paenibacillus polymyxa]
2LAB_A	1.73e-23	797	890	4	102	SolutionStrucuture of the CBM25-2 of beta/alpha-amylase from Paenibacillus polymyxa [Paenibacillus polymyxa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P30269	4.00e-139	65	762	138	881	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P00691	7.23e-135	50	693	25	652	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	4.62e-89	70	875	49	758	Alpha-amylase OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=amyA PE=3 SV=2
P21543	4.09e-46	605	890	365	666	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
A0P8X0	2.06e-28	700	891	903	1187	Alpha-amylase OS=Niallia circulans OX=1397 GN=igtZ PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.019499	0.975387	0.004251	0.000296	0.000268	0.000271

TMHMM  Annotations     

start	end
12	30