CAZyme Information: MGYG000001514_05253

Basic Information

• Species: Paenibacillus_A ihumii
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A ihumii
• CAZyme ID: MGYG000001514_05253
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
941		102481.92	4.9457

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001514	5923787	Isolate	not provided	not provided

• Gene Location: Start: 4100452; End: 4103277 Strand: -

Full Sequence      

MFKPFQKMIAVWLSLVFVAASLFTNPWSAENEAYAQPGPELQAANGQGRAVASSNGIFSW
DNANVYFVLTDRFLDGDSSNNNSYGRPQRDATGKNIGTFHGGDLKGLTQKLREGYFTDLG
TNVLWISAPYEQMHGWVGGGSGGDFAHYGYHGYYALDYTMMDRNMGTVSDMREFVDLAHS
QGIRVVLDVVLNHPGYSTLQDMEEYGFGARNGVGAGWTPGSGQTWHSFHDRIDYNNSSAW
SGWWGNWVRAGIAGYENCGGSDLTQCVGNLPDFRTNETGNVGLAPILRTKWAKETAGYEA
WIVPAAHSLRKDLGLAPADHLVKMLAAWVEEFGIDGFRADTAKHVELSRWKQLKNESSAA
LQRWRQNNPNKPGADWRDDFWMTGEVWGHGVGKSEYFNYGFDSVINFSFQDSNLNALEGT
YADYASKINSDPGFNVLSYISSHDTRLYDRSRLIQAGSALLLLPGGVQTFYGDEAARAFG
DTGSDPQQGTRSSMNWSSLNREVLSHWQKVGQFRSRHLAVGAGSHAKIADAPYTFKRTYA
KDGIEDRVVVVMGASGTTRVNVSSVFADGSTVRDAYTGNEAVVAGGFAAFTAHANGLILI
EQAAESNLPVVSAAPAGGSFETDSLTVTLHVLKAESGKYTLDGSDPSQGVPYADGTEINI
GSDLAFDESVTLRLYAVNEEGAAVQRYSFTKKNPDAGLTIYFKKPADWGAPSLYYYNTAP
KTAEPTWATAPAMTKVSGDWYSYKIDGVDSAQVIFKDNSGRQHPGQNQPGFVRTADGWYD
GSQWHDSNPDGTGHPGTGGNKVTVYYKHGFTMPYIHYRPEGGTWTAVPGVAMEASGVPGY
SKYTVDIGTASRLEACFTDGRGNWDSNYARNYFFPSGTWTYNGNGQIVQGAPVPLGSTLN
LDIQEALESRGLQLLPGVEHPEAADEELPLEDEQDAGAEVA

Enzyme Prediction     

EC	3.2.1.98	3.2.1.1	3.2.1.-	3.2.1.60

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	102	474	1.2e-147	0.9944444444444445
CBM26	699	771	1.7e-20	0.9333333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	0.0	58	551	185	678	alpha-amylase; Reviewed
cd11339	AmyAc_bac_CMD_like_2	4.28e-40	64	517	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.
cd11320	AmyAc_AmyMalt_CGTase_like	3.65e-34	65	514	7	387	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.
cd00551	AmyAc_family	2.95e-33	65	471	2	252	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	1.93e-32	63	544	1	477	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AZK49196.1	0.0	53	893	124	963
QQZ60411.1	0.0	58	892	60	987
QMV43648.1	0.0	58	901	48	992
CQR56565.1	0.0	58	870	60	967
ASA20374.1	0.0	3	895	7	986

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2LAA_A	8.43e-35	799	892	4	102	SolutionStrucuture of the CBM25-1 of beta/alpha-amylase from Paenibacillus polymyxa [Paenibacillus polymyxa]
2LAB_A	1.38e-33	800	892	5	102	SolutionStrucuture of the CBM25-2 of beta/alpha-amylase from Paenibacillus polymyxa [Paenibacillus polymyxa]
2C3G_A	2.92e-33	696	789	5	97	ChainA, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3H_A Chain A, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_B Chain B, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_C Chain C, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_D Chain D, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_E Chain E, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_F Chain F, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_G Chain G, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_H Chain H, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans]
5A2A_A	5.84e-27	59	579	5	425	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	9.44e-27	59	579	39	459	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	1.04e-155	49	551	175	671	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
P21543	1.01e-31	677	901	428	673	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
A0P8X0	1.87e-31	799	898	902	1001	Alpha-amylase OS=Niallia circulans OX=1397 GN=igtZ PE=1 SV=1
P06547	1.03e-28	790	892	455	558	Beta-amylase OS=Niallia circulans OX=1397 PE=3 SV=1
Q05884	1.62e-22	97	586	93	593	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 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
0.012770	0.985716	0.000361	0.000460	0.000350	0.000314

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001514_05253.