CAZyme Information: MGYG000002963_00919

Basic Information

• Species: Anaerosporobacter mobilis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Anaerosporobacter; Anaerosporobacter mobilis
• CAZyme ID: MGYG000002963_00919
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1080		118929.39	4.8123

Genome Property

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

• Gene Location: Start: 196405; End: 199647 Strand: -

Full Sequence      

MQKTRKMLISLFVVLVVLFQSTINAFAMDNTAVQTQQTSTQVTSAVQATSEADASTFSWD
NATVYFALTDRFSNGDTSNDHSYGRELNQNGKVYSNYMSEPATFHGGDLKGLTKKVNEGY
FTKLGVNAIWITAPYEQIHGWLGADSFRHYAYHGYYTLDYTNVDANMGTAGDLKTFIDTA
HENGIRVVFDVVMNHAGYATLKDMNDFNFGSLTSNWKDYYYSASTNAHWSKDYLYMNKDS
TNWGNWWGNAWVRASQGFNGYTGSESGDDLTMCLAGLPDFKTETSNDPGIPKLLENKWKS
EGRYNQEVAELNKFFSTSGLNRQVSNYQVKWLTDWVREYGVDGFRVDTAKHVQQDVWKTL
KEQSVIALKEWKANNPDKALDDLDFWMTGEAWGHGVSASSSYFSNGFDSMINFGFQGVPA
NMSSLETTYSNYANVINSSSSNVNYLSYISSHDTSTYNRSDLINGGTALLLAPGAVQIFY
GDETARPLDYLNCTYTDQKYRSDMNWNSVNQNVLAHWQKMGQFRDNHIAIGAGQHKLINS
APYTFSRTYDEKGITDGVIVVIGANGATTVDVSSVFGDGSLLTDYYTGAQARVSNGKVSF
TAGTNGVILIEGMNNQPSVWIDQTQGGFYTDAMTVSMNFKNADTATYSLNDSEAVEYASG
DTITFGEAATFGTVFTLKLMAKNTDGITITKTYTFTKEDPDQVLTVHYYKPSSWGTPNIY
YYDEEVSPKKEGNAWPGVGMTNEGDGWYAYSIPLWKEASVIFNYSGNQIPGAKQAGYRVT
TESWIKAGVIYTQNPDNPAPIVSIDAKEGDFYTDALTITPTLTNAVTASYTVNGSSATNL
VSGDKIVIGQGAAVGTTFVLEIKAVNANGTTSKTYTFTKAEEPKENTFTVHYYKPSSWGT
PNIYYYDETVSPKKEGTAWPGTAMSSEGDGWYSYTITGLDKAYVIFNSNGSQTPESGKTG
YLIKADSWIKEGVITTEKPGSKLIPVTFVIKNATTNLGQDVYIVGNIAELGSWNTANAIK
TTISEYPTWTVTVNLPAGETIQFKGIKKDSNGKVVWESGSNHTYTVPSTGSGAVTVNWSN

Enzyme Prediction     

EC	3.2.1.98	3.2.1.60	3.2.1.-	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	107	484	3.9e-151	0.9972222222222222
CBM20	984	1071	3.1e-30	0.9666666666666667
CBM26	889	955	3.3e-22	0.8933333333333333
CBM26	705	773	3e-19	0.92

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	0.0	50	561	178	678	alpha-amylase; Reviewed
cd11339	AmyAc_bac_CMD_like_2	4.19e-44	63	527	4	344	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.
cd11338	AmyAc_CMD	2.87e-37	70	533	10	387	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.
COG0366	AmyA	1.72e-36	62	483	1	355	Glycosidase [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	3.48e-35	63	480	1	253	Alpha amylase catalytic domain family. 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; and 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 this 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
CDM67955.1	5.97e-314	42	1053	54	1086
AGF57034.1	1.64e-296	57	967	70	999
QGH23627.1	6.42e-292	38	963	21	965
QGH27673.1	6.42e-292	38	963	21	965
QUF82981.1	9.07e-292	38	963	21	965

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	3.63e-29	59	597	6	433	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	6.24e-29	59	597	40	467	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis],5A2C_A Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
4CGT_A	1.04e-27	64	608	17	470	ChainA, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans]
1CGT_A	2.47e-27	64	608	17	476	ChainA, CYCLODEXTRIN GLYCOSYL-TRANSFERASE [Niallia circulans]
6CGT_A	4.32e-27	64	608	17	476	ChainA, CYCLODEXTRIN GLYCOSYLTRANSFERASE [Niallia circulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	7.35e-140	51	561	177	671	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
P19584	7.90e-29	907	1080	392	551	Thermophilic beta-amylase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 PE=1 SV=1
P30920	1.54e-26	64	608	51	510	Cyclomaltodextrin glucanotransferase OS=Niallia circulans OX=1397 PE=1 SV=1
P31747	2.69e-26	64	596	51	500	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 6.6.3) OX=29335 GN=cgt PE=3 SV=1
P14014	4.70e-26	64	605	51	509	Cyclomaltodextrin glucanotransferase OS=Bacillus licheniformis OX=1402 GN=cgtA PE=3 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
0.000686	0.998309	0.000227	0.000286	0.000223	0.000203

TMHMM  Annotations     

start	end
7	26