CAZyme Information: MGYG000002395_01507

Basic Information

• Species: Bifidobacterium adolescentis
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium adolescentis
• CAZyme ID: MGYG000002395_01507
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1460	MGYG000002395_1|CGC23	155547.71	6.0323

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002395	2173720	Isolate	China	Asia

• Gene Location: Start: 1775490; End: 1779872 Strand: -

Full Sequence      

MRLSTHTFAGMANALTRKEPPHDDQPELMTRAERRRAARKARAAKTWKKVAAGTVAVATL
FGGMGVASTALAADRDSYQDTIGNPSFESARNQYGLTKHMKNGAILHAWMWSFKTITQHM
PEIAAAGYTSVQTEPMSKIKEVAANGKKFTENWYYVYQPANTSIGNFVVGTEADLKEMTA
TAHKYGVRVIVDVVANHFTSDWNAIDPDWQNKDYFHKRTGCDGPNGEINDYSNRYKVTQC
HLLGLWDLNTQNQAVADRMQKFLKTAVADGVDGFRYDAAKHVELPTEVFDNKQSNYWNTI
LKNGSQFQYGEVLQGDSGLDYKAYANMFRDNSSDGGGNTASNYGKTIRAAVGSNNLDVKM
VKNIDTGGASEDQLVTWVESHDNYANGDKESTGLTDYQIMMGWAVVGSRRAGAPLYFNRP
KGSGGTNPQFAEQSQLGDAGDDMWKNKSVAAVNHFRNAMDGKGENLQNCGDKSCLMIERS
TSDGIQNDGVVIANMGGDKSLSGMDTTLDDGAYPDEVNGGQLVVSNHKIVSGTAKGGAVS
VFYVKGESDPNVSVEAASKEFSSDNVKVTLRAQDADNLKYATTEGESGSFTDGRVISVGN
TLSVGETATVKVTGTAAKDGKKVKKGQALSASVTVKKVEVPPQNLAAQYSTNKVGNGVKK
TINFTSGKGASIADWDSSMLIAQGAANDDPRVYRPNSMYEVPIDLYALYGAYDDDNLYLM
WEMTNVQDVVDTGDDYPLSQGHLWQTQNLPFHIAIDTKDDSTRVDNNGGLKTGGSLWASN
ITWGGEQKLNNVVTISTNGSNGPWIYKGDETGLNANAAYGPAANAKTNTKKSGIKFGYGN
GILSKDVIGIDGGWGESNGRVIGDMKAENQDKAKWVNFNEKGHNSAQMDDHYEIAIPLEE
IGTTADRIASNGIGIELAATFGLSAMDSLPYDLAMNDNADLPDTGSQVNNSFEKSDDDMF
SVKMANIGGEEPPVETKSVKIDQSDYSVDLSEGVATKQLTATTDPKGASVSWSSSDKDVA
TVSPKGVVTPRKAGKATITAKSGTKTSSITVTVTGELPPDPVAKNTVYASKPSGWGKIYA
YVYTGDGATAANNAAWPGVEMTAPSATDGCQQTDLYKYVVPDNLAKGAKVIFNDGGSQQY
PGSRQPGLDYNGGIVKWDGSSAALGAVECETTIPVTSVSISGDGVSGGKLSLKSGASVQL
TATVKPDDATDRKVTWTSSDSSVANVMGTGVVTAGSKAGKATVTATAGGKSASVEVTVEA
VGKQPMTVWYKPASSWTTVKVNWRLGSANAKDATVSMSKACGGWYKYTIADTKGKQVRVT
FTDGKAWDSLDGKGYWASGTVMSVSGGKVSTTAPDCQASAQPMTVWYKPASSWTTVKVNW
RLGSANAKDATVSMSKACGGWYKYTIADTKGKQVRVTFTDGKAWDSLDGKGYWASGDSMA
VAGGQLITDVTPNCTVTNKQ

Enzyme Prediction     

No EC number prediction in MGYG000002395_01507.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM74	649	966	7.8e-151	0.9967948717948718
GH13	111	388	8.4e-105	0.9924812030075187
CBM26	1066	1144	3.9e-20	0.92

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	1.23e-157	103	466	2	352	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.
cd11317	AmyAc_bac_euk_AmyA	1.57e-27	103	383	2	238	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.
cd11320	AmyAc_AmyMalt_CGTase_like	1.04e-24	113	382	46	313	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.
cd11319	AmyAc_euk_AmyA	1.48e-22	112	316	41	235	Alpha amylase catalytic domain found in 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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.
pfam16738	CBM26	7.43e-17	1067	1143	1	67	Starch-binding module 26. CBM26 is a carbohydrate-binding module that binds starch.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AJE06470.1	0.0	29	1460	1	1432
AZH71984.1	0.0	1	1459	9	1462
QHB63356.1	0.0	1	1459	17	1470
AXR42241.1	0.0	1	1460	9	1531
AII77046.1	0.0	29	1361	1	1335

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DC0_A	5.29e-102	100	543	3	420	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1UA7_A	2.61e-101	100	543	3	420	ChainA, Alpha-amylase [Bacillus subtilis]
1BAG_A	7.47e-101	100	543	6	423	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
2TAA_A	7.13e-15	112	457	41	370	StructureAnd Possible Catalytic Residues Of Taka-amylase A [Aspergillus oryzae],2TAA_B Structure And Possible Catalytic Residues Of Taka-amylase A [Aspergillus oryzae],2TAA_C Structure And Possible Catalytic Residues Of Taka-amylase A [Aspergillus oryzae]
7P4W_A	1.64e-14	112	457	41	370	ChainA, Alpha-amylase [Aspergillus oryzae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	9.91e-102	86	599	32	525	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	4.20e-66	96	578	47	502	Alpha-amylase OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=amyA PE=3 SV=2
P30269	5.67e-65	81	583	126	651	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
O77020	9.50e-20	105	383	33	311	Alpha-amylase-related protein OS=Drosophila auraria OX=47315 GN=Amyrel PE=3 SV=2
O77019	1.26e-19	105	383	33	311	Alpha-amylase-related protein OS=Drosophila bakoue OX=30018 GN=Amyrel PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.988105	0.011349	0.000210	0.000041	0.000040	0.000239

TMHMM  Annotations     

start	end
50	72