CAZyme Information: MGYG000000353_02070

Basic Information

• Species: UBA7173 sp900548705
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173; UBA7173 sp900548705
• CAZyme ID: MGYG000000353_02070
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
969		106351.51	5.1018

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000353	2738445	MAG	Sweden	Europe

• Gene Location: Start: 3627; End: 6536 Strand: +

Full Sequence      

MKLKRNSSYGVGALCAAMLLAGSASAAAGDASLDRLEIKLDGKNIISSFNKNQLNYEITL
GEDAATTATFSASPSSASSVLDININGVNCHNHSVGSLMGGENMIKYVVKNGSDSKVYTI
KITTPMVARKEYFTWKNANMYFVFTDRFYNGDTSNDNSYHRKRLSGAADVATFHGGDIKG
LTQKLDYLDKLGINSIWITAPYEQMHGWTGGKNDAFPHYAFHGYYALDWTYMDRNMGTIA
DMKNFVTEAHKRGIRVVMDIVLNHTGYCTLDDGVDYDFGNFNGTPTAGWLPSGTPYSMWA
SQNDVSFNADTQGKWGNWWTGWVRAFSDHDWYQSAGFATAGNDDHTMSLAGLPDVVTEKT
SAVEIPPFLQQKWNAEKGGDYDAYRLPNLESWRQGGKGAPADYIINWLAGWVEYFGIDGF
RCDTAKHVELSRWNQLKEACRKALKNWRESDRADEYAKAWTDDFWMTGECFGWQHGDTGY
FNEGGFDSMINFAFNSSEGSSGRTPTTEDWKYYANFCNGSNGRQVLNYVSSHDTGLHRPG
DQKKVATMFLLCPGGAQIYYGDETSRGYISGCPDQSMSTRSDFNWDAVDNDDNKHWQIIG
QFRRRNPAVGAGTQTELGSDTYARKFSADGYTNAVVIKLNTQAGQTYSVSVGDAFRDGQR
VMDGYNNNTVAAVSGGKVSMKASGPVLLIEEFGSIGGGGGYVDPGEIKPEISASPNGGDF
VDEVTVALSVNPIGTPIHYSTNGTATASSPVYTEGLTFTESTTLSVFASNSAGSTTQEFK
FNKVEAPVPGQAKVSSKPADGATFQDEITVELSVNPAGVPIHYAVNGTATASSPVYTKPL
KFTETTTLSVFTDNEGVTNTQSFTYTKTDLPPQPEVYVLLKNTANWSNPTVWAWVDDNNN
SVKAEKWPGDAMIKDGDYWRWELPEGKTTPKFIIFSNNGGSQTKNLDFVNKQIYDCNGNK
VNGDVPTRR

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	176	564	3e-120	0.9972222222222222

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	8.49e-167	133	622	185	663	alpha-amylase; Reviewed
cd11339	AmyAc_bac_CMD_like_2	1.05e-48	139	606	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.
cd00551	AmyAc_family	1.91e-35	140	560	2	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.
COG0366	AmyA	6.60e-34	138	563	1	355	Glycosidase [Carbohydrate transport and metabolism].
cd11340	AmyAc_bac_CMD_like_3	9.50e-34	140	563	6	352	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALA51229.1	9.35e-163	133	942	27	819
BAD64146.1	1.40e-162	133	942	42	834
CAA39096.1	3.89e-162	133	942	42	834
AST98710.1	4.00e-162	133	942	42	834
QNM45711.1	4.00e-162	133	942	42	834

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4E2O_A	1.05e-27	130	617	2	376	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
5A2A_A	6.37e-26	134	563	5	327	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	1.01e-25	134	563	39	361	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]
6SAO_A	5.76e-24	135	689	6	436	Structuraland functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Thamnidium elegans]
5OT1_A	1.08e-20	137	609	290	690	ChainA, Pullulanase type II, GH13 family [Thermococcus kodakarensis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	7.22e-120	133	617	184	651	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q05884	9.35e-31	169	654	91	563	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P21543	5.45e-28	135	675	744	1180	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P38536	2.31e-19	99	693	357	924	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P36905	2.64e-19	136	693	387	925	Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2

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
0.000348	0.998863	0.000238	0.000197	0.000182	0.000163

TMHMM  Annotations     

start	end
7	29