CAZyme Information: MGYG000000510_00333

Basic Information

• Species: UMGS363 sp900541495
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UMGS363; UMGS363 sp900541495
• CAZyme ID: MGYG000000510_00333
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
552	MGYG000000510_4|CGC1	61722.73	4.2586

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000510	2415256	MAG	Fiji	Oceania

• Gene Location: Start: 2920; End: 4578 Strand: +

Full Sequence      

MKKTPFSISAAAAVTAAAILLSGCGTPEETMSDSLQPQTPAYQYDHELNVIDDNYRNYYQ
VFVYSFCDSNGDGIGDLAGVTSRLDYIQDMGFNGIWLSPIMPSDSYHKYSVKDYYAIDEQ
YGTMEDFEELAAECRKRGIKLLIDLVMNHSSNKHEWFTLASQSLRSDPCGAAKDEPCLND
NVCPVHDPYIDYYYFADEKPVGTNSWYQTGSYWYQAVFSENMPELNLDNPAVRGEFEKIA
DFWLEKGAGGFRLDAVKEYFSGNPDKNIEVLEWFMKHCKAADPECYVVGEVWESFTTYTK
YYSSGIDSVFGFTMAQEDGKIAKTINMSGADNSVKSFAQAMTTIEQKLASYSDTAIDAPF
IGNHDTNRGAGIFRYDETKIKAAAGLLLTMSGSPFVYYGDEIGLSGSGRDENKRAPMIWD
SEGTGLTYGPPNMERQENRFADVQMQLADENSILNYYKRALRIRNENPCIARGTTEVITV
PGQDIAAVRRTWDGDSIVIVYNYSGESRDVTEIDGLSDMQIRGYLTVDSAQEVLLDGGLT
MPAYSIAFLTEK

Enzyme Prediction     

No EC number prediction in MGYG000000510_00333.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	75	406	5.5e-112	0.9936305732484076

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11316	AmyAc_bac2_AmyA	0.0	56	473	1	403	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.
cd11333	AmyAc_SI_OligoGlu_DGase	1.03e-107	59	466	6	428	Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins. The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. 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 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	8.91e-84	58	473	4	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	1.37e-81	59	511	4	491	Glycosidase [Carbohydrate transport and metabolism].
cd11331	AmyAc_OligoGlu_like	1.20e-79	59	474	9	450	Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. 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
CBL34098.1	0.0	1	552	1	553
CBK95784.1	0.0	1	552	1	553
CUH92222.1	3.17e-185	27	549	40	572
BCN32943.1	2.94e-180	42	549	42	560
BCJ92468.1	6.44e-176	42	549	10	526

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7JJN_A	3.86e-138	49	552	28	524	ChainA, Glycosidases [[Eubacterium] rectale DSM 17629],7JJN_B Chain B, Glycosidases [[Eubacterium] rectale DSM 17629]
7JJT_A	1.17e-98	53	549	27	520	ChainA, Alpha-amylase [Ruminococcus bromii]
1WZA_A	6.82e-90	53	502	2	438	Crystalstructure of alpha-amylase from H.orenii [Halothermothrix orenii]
2PWG_A	5.66e-64	58	516	11	521	ChainA, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],2PWG_B Chain B, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],2PWH_A Chain A, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],2PWH_B Chain B, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila]
1ZJA_A	5.78e-64	58	516	12	522	ChainA, Trehalulose synthase [Burkholderia ubonensis subsp. mesacidophila],1ZJA_B Chain B, Trehalulose synthase [Burkholderia ubonensis subsp. mesacidophila],1ZJB_A Chain A, Trehalulose synthase [Burkholderia ubonensis subsp. mesacidophila],1ZJB_B Chain B, Trehalulose synthase [Burkholderia ubonensis subsp. mesacidophila],2PWD_A Chain A, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],2PWD_B Chain B, Sucrose isomerase [Burkholderia ubonensis subsp. mesacidophila],4H8V_A Crystal structure of the trehalulose synthase MUTB in complex with trehalulose [Rhizobium sp. MX-45],4H8V_B Crystal structure of the trehalulose synthase MUTB in complex with trehalulose [Rhizobium sp. MX-45]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20845	5.87e-94	58	506	42	482	Alpha-amylase OS=Priestia megaterium OX=1404 PE=1 SV=1
P14899	1.98e-88	55	502	32	454	Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC PE=3 SV=2
Q54796	7.87e-60	59	542	12	526	Glucan 1,6-alpha-glucosidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=dexB PE=3 SV=2
Q9K8U9	6.77e-55	59	509	12	516	Oligo-1,6-glucosidase OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=malL PE=3 SV=1
P29094	1.30e-53	59	504	12	512	Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000001	1.000045	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000510_00333.