CAZyme Information: MGYG000001076_00996

Basic Information

• Species: CAG-411 sp000437275
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-411; CAG-411 sp000437275
• CAZyme ID: MGYG000001076_00996
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1517		162312.42	6.6581

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001076	3627630	MAG	Sweden	Europe

• Gene Location: Start: 14648; End: 19201 Strand: -

Full Sequence      

MVRKKVLSIALAAMMTTGTILGDNSALYQSIFVKAKTTTDTEVTVDEKQVDANEYGLVDN
IQDGTILHCFDWKYNDIKAELKNIADAGFTSVQTSPAQRDDSYGVWYMLYQPQSFSIATN
ALGSKEDLQSLCTEAEKYGIKVIVDVVANHMRGDGNNVDDNMKRSNHPDYWHTDDYDSGR
NIDWKNRFQVTHGRIGMQDLNSENSSVQNIVANYVKELASVGVDGIRWDAAKHISLPSEN
CNFWKVVTEAAGLYNYGEILGGPTDDTSSESAKSLMKEYINYMSVTDNSYGSDLCGSFRD
GKITGTSGIWTNKGVSADKLVYWGESHDTYANDEGDGGWTKNISQNAVDRAYAIAAGRAD
ATSLYFSRPSATAKTSIMAGAKGSTHFTSKEVAAVNHLHNACVGQKDYYVAGSDAAAVCR
ETGAVIVKGSGSGQVTIQNGGGLTAPGTYTDEVSGSTWTVTADTISGTVGDSGIAVIYNG
AKKPTVSVSKDSGTFTEPFELTLTPSNVDKATYSINGGDAVEFTKATKVKIGEGCQIGDK
VTVKITATGEGESFEKTLTYTMTDVPVAKFLVRAKKSDFTSAPYIYAFSSGATAKEYAGK
WPGTKMTEEGDYYVFSSDDMDSATVILSDGNNGWRNTQENETEVVVNGMMEYDKSSNKFT
TITIASKTPSPTTVVTPTPKITETPKVTETPKITETPKATVNPTPTVTAESKVSIDVSLD
SGSSFTTESKDVKVTLKNATSGTYRVDNGPVKTFTGSATVTIGQGKIADTDVTLEVTAIS
GKNELTKTFTYHKVFDGTTAQVKTAAVTKIQSLLEVVAEAAQANTAAESDAYYATNPGSK
VGKKASIEIDGSFSDWSDDMLIAQGAAFDTATAFKGQWENCVMDSYSLYGAWDDENLYIG
FQLVNVYDDALKDSGMDLAGGPLSCNGKIGDLLITIAINTGKGNAMTGRVSDGKGIWGQE
IEFKTRVDNILVFHGDNTGTPGFFTGTEDGTTNYKANCQNFKELGIEVESADGCLPKTIM
GVKDNQGDVQASYSMDSAWIDFNTTTHDNKYDTFYEVKIPFSALGITASDVENNGVGVMQ
LIGRGESGMDCIPHDPSMLDNTMGDYAAQPTNSHEKDDTDIITVPLAAIGNMKATGEGSG
GNVSTPKPSTATTEPQKTEVVKTPAATEKATPKATTPAQTIKPTAKVTATPVQTKKPATA
EPVATSNPGKKFTVNFGADRSSPQYDSTKLVLKAIPYGASGDCKYEFLVDGETVQKASKN
ATYTWNGTEGKHTIKVVVEDASGNKISSEKQYVIEHSGTATPVVKPTATASIEDPKNTAT
PGVEETAQPLSARIKLSAASPQKVGKRVTLQLIANGGTAPYKYSVTATKSNGKKTTLLKN
SNKSTVVWTPANAGTYKLTATIEDANGVKAVKNVTYTIKVVSPIKVKTFKVSKYSIARGK
SVKITVKATSSNKGKVKYKISVQKKGDAKKTVVRKYSTKTTYTWKASKKGKYTIYITVRD
AKGKTTTKKLSKQITVK

Enzyme Prediction     

No EC number prediction in MGYG000001076_00996.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM74	833	1127	6.1e-73	0.9935897435897436
GH13	72	334	1.2e-69	0.9924812030075187

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	1.57e-112	63	409	1	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	1.29e-35	64	342	2	251	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.
cd11319	AmyAc_euk_AmyA	5.29e-25	84	287	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.
smart00642	Aamy	1.21e-19	65	159	2	103	Alpha-amylase domain.
COG0366	AmyA	4.81e-17	57	261	7	241	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDM67953.1	2.13e-177	49	1464	35	1319
AWX97480.1	1.01e-155	25	1314	3	1175
AWX95531.1	1.39e-155	25	1314	3	1175
QFJ55411.1	2.05e-138	44	477	37	464
QNT67433.1	6.53e-122	53	601	26	571

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DC0_A	2.65e-65	60	478	2	420	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1UA7_A	6.51e-63	60	478	2	420	ChainA, Alpha-amylase [Bacillus subtilis]
1BAG_A	1.30e-62	60	478	5	423	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
1G94_A	2.96e-19	65	338	4	271	CRYSTALSTRUCTURE ANALYSIS OF THE TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS IN COMPLEX WITH A HEPTA-SACCHARIDE AND A TRIS MOLECULE [Pseudoalteromonas haloplanktis],1G9H_A TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA-AMYLASE, COMII (PSEUDO TRI-SACCHARIDE FROM BAYER) AND TRIS (2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL) [Pseudoalteromonas haloplanktis],1L0P_A Crystal Structure Analysis Of The Complex Between Psychrophilic Alpha Amylase From Pseudoalteromonas Haloplanctis And Nitrate [Pseudoalteromonas haloplanktis]
1JD9_A	3.08e-19	65	338	4	271	ChainA, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	1.39e-71	60	649	46	647	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	1.83e-56	57	484	47	467	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	2.94e-37	59	477	143	605	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P41131	1.47e-22	63	328	25	288	Alpha-amylase OS=Aeromonas hydrophila OX=644 GN=amyA PE=3 SV=1
P29750	3.61e-21	66	329	42	314	Alpha-amylase OS=Thermomonospora curvata OX=2020 GN=tam 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
0.001794	0.997159	0.000244	0.000292	0.000242	0.000227

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001076_00996.