CAZyme Information: MGYG000004255_01597

Basic Information

• Species: Amulumruptor sp900547825
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Amulumruptor; Amulumruptor sp900547825
• CAZyme ID: MGYG000004255_01597
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
694		74813.82	5.2704

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004255	2427013	MAG	China	Asia

• Gene Location: Start: 19584; End: 21668 Strand: +

Full Sequence      

MTALLALPVTGVAAGSYGLPDGIQQGNILHCFNWPISEVKASLPSIAAAGFGSVQLSPLQ
RGDIRTGSSWHDLYRPYDLAFKSSSFCSEQDLKSLCEEAATYGIKVIVDVVANHVDKTAG
YHDTWWDANGRVRWEGGINYGDRNSITHGQLGDYGDINSESAEVCARGKAYVEKLKSLGV
KGIRWDAAKHIGLPSEGCNFWSSVTSVSGMYHYGEILNEPGPNENIIKEYAQYMSVTDNR
YSNGAARDNGGIPQGYGGAWVVNYSVPDTKVVYWGESHDTYSNDEWSQNVDQSVIDRAYA
SFACRNGATALYLARPKTKGFSNIKVGKGTTAYEGKHIAAVNKFRNAMTGRADWCEANGN
TFCVTREDGGAVIVMKGSGNVSVTNGGGYCPAGTYTDMVNGGKFTVTATTISGNVGSSGI
AVIMKDGVGPNPNPDPNPDPNPNPNPESVTITGDYNLAYNGSKSNVYYWATGNSPIAWDD
APAMASVKGSDGNTYKVYKLPAGMTNVIFKDGSGQTDDLDYTSQYVMNDNGATTTKVIFK
NGNNPGPDPIEGGWNAYFKNSANWGSVYAYVWDANEAGSDSKYFGAWPGKKLELDAVSGY
FKASVAIDNAAGKKMMIIFTDNSGNQTDDLEFKNNGIYDLTGHIGEYSSFIQSIGTDENL
PAVYYNLQGIQVENPTNGIYIERRGKKARKVVIR

Enzyme Prediction     

No EC number prediction in MGYG000004255_01597.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	34	285	6.7e-49	0.9924812030075187
CBM26	556	632	4e-17	0.9466666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	1.54e-78	25	352	1	349	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	1.00e-18	28	280	4	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.
pfam16738	CBM26	4.03e-12	557	630	2	67	Starch-binding module 26. CBM26 is a carbohydrate-binding module that binds starch.
cd11319	AmyAc_euk_AmyA	2.61e-11	46	238	52	251	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.
cd00551	AmyAc_family	1.50e-09	19	303	6	240	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
QUB83913.1	1.51e-105	23	425	31	435
QFJ55411.1	2.03e-104	9	535	38	599
QNT67433.1	9.49e-98	13	664	24	651
QCT06294.1	2.39e-61	13	623	46	646
AWQ15645.1	2.54e-59	21	642	45	652

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UA7_A	5.25e-54	23	426	3	422	ChainA, Alpha-amylase [Bacillus subtilis]
1BAG_A	1.49e-53	23	426	6	425	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
3DC0_A	9.67e-53	23	426	3	422	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1UKS_A	1.33e-12	74	543	100	609	ChainA, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1UKS_B Chain B, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011]
1UKT_A	4.03e-12	68	543	95	609	ChainA, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011],1UKT_B Chain B, Cyclomaltodextrin glucanotransferase [Bacillus sp. 1011]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	3.89e-56	23	645	47	655	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	3.17e-41	19	513	47	549	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	2.77e-35	21	631	143	777	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P54215	1.55e-16	3	423	6	475	Alpha-amylase A OS=Drosophila mauritiana OX=7226 GN=Amy-d PE=3 SV=1
Q23835	2.73e-16	3	423	6	475	Alpha-amylase 1 OS=Drosophila ananassae OX=7217 GN=Amy35 PE=3 SV=3

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
0.653717	0.345366	0.000260	0.000304	0.000157	0.000204

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004255_01597.