CAZyme Information: MGYG000003835_00212

Basic Information

• Species: UBA7173 sp001915385
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173; UBA7173 sp001915385
• CAZyme ID: MGYG000003835_00212
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
983		107142.54	4.627

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003835	3225656	MAG	United States	North America

• Gene Location: Start: 13080; End: 16031 Strand: +

Full Sequence      

MNIRNISHKVSAAVAMMLLGTAFTATGAAVNSGDATLSALEIKVDGQNLVNFDRNTTSYS
IELDDTSLMTLSAAPTASDATVTITVNGREYDNHSLASLDGGENTIVYNIVSGTASQAYT
IKIKTPQVLRGRHFSWKNATIYFVLTDRFYNGDTANDMSYHRQRSQGNMPDYATFHGGDI
KGLTEKLDYLNRLGVDAIWISAPYEQMHGWTGGKGDAFPHYAFHGYYALDWTYMDRNMGT
VEEFRSFVTEAHKRGIRVVMDIVLNHTGYCTLDDCVDYDFGNFNGTATAGWMPSNGNYTM
WSDDNEVSFNADTQGKWGNWWSGWVRAFGDRSWSSSAGFAPGGGDNFTMSLAGLPDVVTE
KTSAVNIPPFLKLKWEQENSGDYLDYRLPNLDAWRTDGKGAPADYLIAWLAGWVEEFGID
GFRCDTAKHVELSRWNQLKQACKTALANWRASSRADEYAKSWTEDFWMTGEAFGWDHGDT
GYFTSGGFDSMINFAFNSSEGSQGRTPSTSDWEYYANYCNGSNGRQVLNYVSSHDTGLHR
PGDQKKVATMFLLCPGGAQIYYGDETSRGYMSGCPDQSMATRSDFNWDAVDNADNKHWQL
IGQFRRRNPAVGAGTQSNLGPDTYGRSFTDGAYANAVVIRLNTSAGQTYTVNVNGFFADG
TKVMDGYNTATTATVDGGKVTMQASGPVLLVEAYGQITDDEIDTPTPPVPPVPQKPVVTA
TPGSSTFSESVTVTLSVNPAGTPIRYSVAGAANASSTVYTSPLTFTETTTLSTYVENEAG
SNVQSFTYTKSDTPGPGPDPDPDPNKQYVYFNNTQNWTPYVWAWNETENCTAAGAWPGDA
MTQKDGKYYWEAPAGKVPTLIIISDKGGTRAGNGNLEYVNGATYNPDGSTGDGPTPPTGD
NVVYFDNGATNWSTVKVHYWGGESASSWPGVNMIVHSGNIYKYTVPSGTTGLVFNNGSGD
QSGNLTFAKGHLYDKNGDKGEYK

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	178	566	9.2e-121	0.9972222222222222

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	1.88e-168	134	616	185	655	alpha-amylase; Reviewed
cd11339	AmyAc_bac_CMD_like_2	7.94e-47	140	608	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	4.60e-36	140	562	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.
COG0366	AmyA	5.67e-34	139	565	1	355	Glycosidase [Carbohydrate transport and metabolism].
cd11320	AmyAc_AmyMalt_CGTase_like	6.24e-34	137	307	3	173	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSI03195.1	5.76e-159	37	692	378	1096
CQR56565.1	1.46e-158	95	849	21	749
QQZ60411.1	8.56e-153	95	849	21	748
ADZ82879.1	1.28e-152	133	869	49	762
CAA37453.1	7.41e-152	129	822	46	712

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	1.51e-26	135	496	5	244	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	2.42e-26	135	496	39	278	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]
4E2O_A	2.71e-26	135	614	6	371	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
6SAO_A	6.35e-21	136	681	6	424	Structuraland functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Thamnidium elegans]
6WNI_A	1.28e-20	137	307	32	210	ChainA, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNI_B Chain B, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNU_A Chain A, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	3.42e-121	134	619	184	651	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q05884	1.17e-29	171	686	91	614	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P21543	4.51e-26	136	663	744	1166	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P36905	7.29e-25	137	696	387	926	Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P38536	1.57e-20	137	696	387	925	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB 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
0.000538	0.998658	0.000200	0.000210	0.000185	0.000165

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003835_00212.