CAZyme Information: MGYG000003550_02416

Basic Information

• Species: Clostridium sp900769625
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp900769625
• CAZyme ID: MGYG000003550_02416
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
666	MGYG000003550_90|CGC1	78369.36	5.6113

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003550	3104477	MAG	Fiji	Oceania

• Gene Location: Start: 20662; End: 22662 Strand: +

Full Sequence      

MIIFLIISIMAAFIFLLIYIYLQIRKRFNDIENQMCNLKKSNNNFDYEIKRIGDEIESLD
EEVCSINVENQKSDTSHESTGEVLDKKKFYIQVDNMIRRYIEINIDRYIGECRKDRKRTN
GHKNLKKIEDNRNIRSHLPEKTTVLDIDKAFQIGIENLKNKKKIEYEISKFKEESGSTEI
KNSKRDNKTMMQFFEWYYHNDGSLWMKVKNEAENLKSIGITSLWLPPAYKAHNGINDVGY
SAYDLYDLGEFNQKGTIRTKYGTKDEYIEAIKEAHRNGIEIYGDVVFNHKAGADGTELVE
ARQVDENDRNVFIGEEKQIRAHTIFSFPGRMEKYSAYKWTANDFDGVDYDDISKQSGIFK
FQGKEWEEDVDKEKGNYDFLMFADLDMDSPYVIEELKRWGKWYMDETQVDGFRLDAIKHI
RFDFFKEWLEEMRNYSRKELFAVGEYWTWDVGRLRYYLDRCGHSMKLFDPPLHYNFYSAS
NSLGYFDMRRIKDNTLLQLEPEYTVTFVDNHDTQLGQSLESWVSPWFKPLAYTFILTREE
GYPCVFYGDYYGIPDKGYEGIKDILDRILSARKKYAYGIQHDYMDDKSVIGWTREGDNTH
KNSGLAALITVACGGKKKMNVGIKHKGEKWIDMTSQNKCEVTIDKDGNGEFYVQDGSYSI
WISKDA

Enzyme Prediction     

EC	3.2.1.1	3.2.1.98	3.2.1.-	3.2.1.41

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	215	553	7.2e-150	0.9941520467836257

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11318	AmyAc_bac_fung_AmyA	0.0	187	574	1	391	Alpha amylase catalytic domain found in bacterial and fungal 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 bacterial and fungal proteins. 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.
PRK09441	PRK09441	0.0	187	662	3	479	cytoplasmic alpha-amylase; Reviewed
cd11314	AmyAc_arch_bac_plant_AmyA	1.61e-54	190	576	2	295	Alpha amylase catalytic domain found in archaeal, bacterial, and plant 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 from bacteria, archaea, water fleas, and plants. 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.
PLN02784	PLN02784	2.45e-30	128	547	427	814	alpha-amylase
COG0366	AmyA	4.67e-25	215	592	38	398	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGH26126.1	0.0	1	664	1	664
QGH22087.1	0.0	1	664	1	664
APF24585.1	0.0	1	664	1	664
AXB85381.1	0.0	1	664	1	664
QCJ07475.1	0.0	1	664	1	664

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4UZU_A	4.05e-209	187	664	5	481	Three-dimensionalstructure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolution [Geobacillus stearothermophilus]
1HVX_A	3.27e-206	187	664	5	483	BACILLUSSTEAROTHERMOPHILUS ALPHA-AMYLASE [Geobacillus stearothermophilus]
6AG0_A	6.81e-205	187	664	32	510	TheX-ray Crystallographic Structure of Maltooligosaccharide-forming Amylase from Bacillus stearothermophilus STB04 [Geobacillus stearothermophilus],6AG0_C The X-ray Crystallographic Structure of Maltooligosaccharide-forming Amylase from Bacillus stearothermophilus STB04 [Geobacillus stearothermophilus]
6GXV_A	3.40e-190	186	664	5	484	Amylasein complex with acarbose [Alicyclobacillus sp.],6GXV_B Amylase in complex with acarbose [Alicyclobacillus sp.],6GYA_A Amylase in complex with branched ligand [Alicyclobacillus sp.],6GYA_B Amylase in complex with branched ligand [Alicyclobacillus sp.],6GYA_C Amylase in complex with branched ligand [Alicyclobacillus sp.],6GYA_D Amylase in complex with branched ligand [Alicyclobacillus sp.]
2DIE_A	5.27e-187	187	664	6	485	Alkalinealpha-amylase AmyK from Bacillus sp. KSM-1378 [Bacillus sp. (in: Bacteria)]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P06279	1.46e-205	187	664	39	517	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
P00692	1.28e-184	177	664	23	514	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
P06278	1.36e-183	187	664	33	512	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
P19571	2.37e-183	187	664	39	518	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
P26613	5.52e-127	187	666	3	494	Cytoplasmic alpha-amylase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amyA 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
1.000018	0.000015	0.000001	0.000000	0.000000	0.000001

TMHMM  Annotations     

start	end
2	24