CAZyme Information: MGYG000001076_01026

Basic Information

• Species: CAG-411 sp000437275
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-411; CAG-411 sp000437275
• CAZyme ID: MGYG000001076_01026
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1590		171084.49	4.9035

Genome Property

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

• Gene Location: Start: 7150; End: 11922 Strand: -

Full Sequence      

MHNIKRRIMGSLMAVLMGTSTILGTCPAPLFAANVSAKAEVEVTSDASEVNANQYGLVSA
KQGNILHAWDWKFTDVTKNIEDIAEAGYSLVQVSPCQVCENTTTNNDWWKLYQPYDYKFG
NSLGTADEFKEMCSTAEKYGVSIIVDVVANHMAGTGTGSCGERKSQVDSWWTDDKFHNTG
VKFTGTYDDNREMMVRSNIGMPDVATEREDVQERMISYLETLLDMGADGFRYDAAKHIGT
TSDSGNSNDTFWKNISAAVSAKKPDALVYGEILNSMPVSDEYYVKDGIKVTESQKGWDMK
DLVRGEGTVSQKSAFTYTRKSSASNLITWVENHDTYLNHWGSTGLADNHNHKNYMSDDQI
MLAWSTVAARADAQALYFARPDGCSEPANPNDNDASNTIQGNLGMSTKNFDWKDKKVASV
NKFKNAMVGEGEECSTSGNLAIIKRGNKGVVVTNFGSGSANFDVSGLSGLKDGKYTDASG
QNGEFTVSGGKVSGSVKGNSFVVLYDADSVVQVTETPSATPDETPVAGAASVSFENGGGK
FKEAVKETITVKNAEYAYYSYDGADWTEIKDGKATVTIGADAKNIGDTYALYVKAMGKDG
KLVDSEKTYTYSTSSSETGTTHSLKLRIAKSEQATAPYVYFKGSTTAWPGEAMTEEGDYW
VYVSDTMTSGEVIFNGGTGSWQDPEKDKGWHTVAGYMQYSLKDKAVTEFSETTEATVSPD
AKKANKAPEFVISTTKPTETPATQTEEPTEAPTATPDNVTGEMSISVNKVDGTQFDTETL
PVTIKVENATDAVYSIDGGAEVSFDGETTVEVGEGKIADTDVTLKVTATDKEGTRSATTY
TYKKVFNPKKAAEEQKVGTVTTAVTKIKSLMEVVSDAAQADADVLQGEPESSYFSTNPNN
QTGAKKTITSAKDFTEDMIIAQGVANDGITSFKGTHEGPVYDTYALFGAYDDTNVYIGVQ
YTNVIDVIDPAQGYPISDNGKPSAGDIPQMMVFDTRSGDYTDGTANDTKQKTAWDTNVKF
AGDAKVDKLFVYSAKAEVNNTALFKSVNGIVDYNTVISSKIASTGKTGITYKYEDGFFCK
NMYGIKRNGYDGYTPADLNSDSSEWIDFLTTSHDTDKDTFMIMTIPMSTLGVTADKVASE
GIGVMSISTFGASGIGSCPQDLSMLDVACDPYGPDESTSAEKEDEDTVTTKLAQLGGSVD
NPIKTPKPITSAEVTATPDSSVATATPEVTPCVTATPEATDSSVATATPEATDSSVATAI
PEVTPHVVATPIVPEDTDQMVVNFGAEKAAPQVAGTTLKLEAKPYNTTGTCQYQFVVDGQ
VVQEYSESASYNWYATSGKHTISVSVKDQTGKYVVVEKNYTVMGDNPATQEPTATPEVTP
CVTATPVQSPTIEDPKETEAPVEITVKASFGKASPQKVNTAIKITPRVSGTKNSYKYSIM
AELKNSTYTQRVASNSTAKSVTWKPKKAGTYKITISVTDSEGYKGVKTYNYVIKQPKLTV
KGSISKKSIKLGQKVKITTNGTASKGTLKFKITSKKKGDKKAVVLKKYSTKKTCIWKPKK
KGTYTITVYAKDGSGKQVKKTLKLTVKAKK

Enzyme Prediction     

No EC number prediction in MGYG000001076_01026.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM74	894	1193	5.6e-84	0.9935897435897436
GH13	71	339	2.4e-67	0.9887218045112782

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	3.38e-95	62	433	1	351	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	3.73e-40	65	364	4	267	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.
cd00551	AmyAc_family	4.56e-19	67	335	20	216	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.
cd11316	AmyAc_bac2_AmyA	4.29e-17	116	288	58	241	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 Chloroflexi, Dictyoglomi, and Fusobacteria. 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.
COG0366	AmyA	5.20e-17	69	405	26	374	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDM67953.1	2.25e-212	28	1586	19	1367
AWX97480.1	3.47e-116	58	1362	27	1158
AWX95531.1	8.57e-116	58	1362	27	1158
QIK84188.1	9.61e-93	65	1196	61	1152
ASR47410.1	3.87e-91	31	675	20	624

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DC0_A	2.94e-71	59	505	2	420	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1UA7_A	2.11e-67	59	505	2	420	ChainA, Alpha-amylase [Bacillus subtilis]
1BAG_A	4.23e-67	59	505	5	423	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
3BLP_X	1.52e-25	64	516	12	482	ChainX, Alpha-amylase 1 [Homo sapiens]
3BLK_A	2.70e-25	64	516	12	482	ChainA, Alpha-amylase 1 [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	8.35e-72	37	678	29	629	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	1.28e-64	59	578	50	531	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	1.13e-56	36	679	119	770	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P91778	6.53e-29	62	500	28	480	Alpha-amylase OS=Pecten maximus OX=6579 PE=2 SV=1
P83053	1.97e-25	64	499	12	477	Pancreatic alpha-amylase OS=Struthio camelus OX=8801 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000526	0.283302	0.712839	0.002682	0.000464	0.000164

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001076_01026.