CAZyme Information: MGYG000001416_02091

Basic Information

• Species: Cellulomonas massiliensis
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Cellulomonadaceae; Cellulomonas; Cellulomonas massiliensis
• CAZyme ID: MGYG000001416_02091
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
485	MGYG000001416_1|CGC29	51478.05	4.1611

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001416	3245988	Isolate	not provided	not provided

• Gene Location: Start: 2264128; End: 2265585 Strand: -

Full Sequence      

MTAARRLAAPLVLAAALALGACTGGPPPLDPEASPAADGTGRDVGVQLFQWTWDAIAAEC
TDHLAPAGYAWVLTSPPQEHIRGEAWWTAYQPVSYRVESRLGTREQYAAMVRTCHEAGVD
VWADAVVNHMTAQDAGVGWAGTRFEHQRYPGLYEPVDFHHCGLTPDDDIASYLDAEQVQT
CELLDLADLDTGSAHVRATIVAYLEDLLGLGVDGFRIDAAKHMAAEDVAAIVGALPEGTG
VAQEVIRGSNEPIQPEDYLGAGQVYEFTYGKELKGVLAGSPRLALTLGEARARYVPSDDA
VVFVDNHDTERNGSTLSYQDGDAYALAQVLMLAGTYGTPQVLSGYAFGDTDAGPPQDEDG
RVRDATCADDVGPARAWADGDWVCQHRWPEVAGMVGWRAAVGDAPVVDAWSDGDAVALGR
GERGFVVVNAGDEPLTATLTTSLPDGRYCDVLVASGCEEARVSDGRVDVVVPPGSARAWD
TAARR

Enzyme Prediction     

EC	3.2.1.1	3.2.1.116

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	68	333	2.5e-96	0.9888475836431226

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11317	AmyAc_bac_euk_AmyA	7.53e-157	42	401	1	329	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.
cd11315	AmyAc_bac1_AmyA	1.03e-47	43	343	2	310	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.
cd11320	AmyAc_AmyMalt_CGTase_like	2.40e-24	71	351	65	360	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.
smart00642	Aamy	2.32e-21	46	132	4	97	Alpha-amylase domain.
cd00551	AmyAc_family	6.76e-15	62	341	32	251	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
AEI11782.1	1.69e-260	5	484	6	486
ASR56787.1	9.66e-254	7	485	15	491
QVI67910.1	1.46e-248	12	484	10	481
VEH33024.1	4.87e-237	19	484	42	498
AEE46444.1	4.87e-237	19	484	42	498

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JD9_A	7.93e-106	46	483	6	440	ChainA, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]
1G94_A	2.71e-105	46	483	6	440	CRYSTALSTRUCTURE ANALYSIS OF THE TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS IN COMPLEX WITH A HEPTA-SACCHARIDE AND A TRIS MOLECULE [Pseudoalteromonas haloplanktis],1G9H_A TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA-AMYLASE, COMII (PSEUDO TRI-SACCHARIDE FROM BAYER) AND TRIS (2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL) [Pseudoalteromonas haloplanktis],1L0P_A Crystal Structure Analysis Of The Complex Between Psychrophilic Alpha Amylase From Pseudoalteromonas Haloplanctis And Nitrate [Pseudoalteromonas haloplanktis]
1AQH_A	3.15e-105	46	483	6	440	ALPHA-AMYLASEFROM ALTEROMONAS HALOPLANCTIS [Pseudoalteromonas haloplanktis],1AQM_A ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS COMPLEXED WITH TRIS [Pseudoalteromonas haloplanktis],1B0I_A ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS [Pseudoalteromonas haloplanktis]
1JD7_A	3.15e-105	46	483	6	440	ChainA, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]
1KXH_A	1.52e-104	46	483	6	440	ChainA, alpha-amylase [Pseudoalteromonas haloplanktis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P09794	4.11e-126	4	484	2	457	Alpha-amylase OS=Streptomyces limosus OX=1947 GN=aml PE=3 SV=1
P30270	3.27e-125	4	484	2	457	Alpha-amylase OS=Streptomyces griseus OX=1911 GN=amy PE=3 SV=1
P27350	1.77e-123	42	478	35	452	Alpha-amylase OS=Streptomyces thermoviolaceus OX=1952 GN=amy PE=3 SV=2
P22998	2.02e-121	3	451	2	426	Alpha-amylase OS=Streptomyces violaceus OX=1936 GN=aml PE=2 SV=1
P08486	3.71e-110	13	483	12	447	Alpha-amylase OS=Streptomyces hygroscopicus OX=1912 PE=3 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	0.000006	1.000046	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001416_02091.