CAZyme Information: MGYG000003119_00260

Basic Information

• Species: Capnocytophaga ochracea
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Flavobacteriales; Flavobacteriaceae; Capnocytophaga; Capnocytophaga ochracea
• CAZyme ID: MGYG000003119_00260
• CAZy Family: GH13
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
469	MGYG000003119_4|CGC1	53602.19	6.4463

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003119	2451559	MAG	United States	North America

• Gene Location: Start: 48549; End: 49958 Strand: +

Full Sequence      

MKYYIYLLAGLLAFSCDKKNNNDNPEPQNTVPLDLTKIDNGNRVMMQAFYWDVTPLGEWW
NTITPKLTEWKANGVDRIWLPPASKGASGGYSMGYDPSDYFDFGEYFQHKTTKTRFGSRA
ELENLISKAHESGLQVIADIVIGHNNGGGKEWNPYRNKETYTLFDETHGNASGRFNRNYE
CFHPNKYATSDEGADFYGEQDLSHKVPYVREELWEKDNSMAKYYKNTMKFDGWRFDYVKS
FGAWVVRDWLKAVGGFAVGELWDGNPETLKKWVDESGASAFDFACFYALEKALDRNKDMH
ELMTDTHPMLRTLRPEKAVTFTANHDTEKDKIADNTIAPDKKLMAYAYILTHSGYPCIFF
SDYENEAFKAKLQKLMLINRSLAVGEEKFHLASNTEYVASRLGNEKSPGLVLFINNSTLP
AKRTITTHWKNKTLMDYSGNSHLLFVTDSDGNVTIQVPANSYTVWSIGK

Enzyme Prediction     

EC	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	66	363	4.9e-134	0.9965397923875432

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09441	PRK09441	3.46e-180	40	466	1	479	cytoplasmic alpha-amylase; Reviewed
cd11314	AmyAc_arch_bac_plant_AmyA	1.96e-108	44	387	1	299	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.
cd11318	AmyAc_bac_fung_AmyA	5.47e-76	42	380	1	390	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.
PLN00196	PLN00196	1.99e-40	31	378	13	365	alpha-amylase; Provisional
PLN02784	PLN02784	3.26e-32	40	366	500	824	alpha-amylase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACU92189.1	0.0	1	469	1	469
QLF50014.1	0.0	1	469	1	469
AVM55753.1	0.0	1	469	1	469
ALC97351.1	0.0	1	469	1	469
ASF41659.1	8.02e-269	1	469	1	469

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1MWO_A	9.58e-110	44	466	11	430	CrystalStructure Analysis of the Hyperthermostable Pyrocoocus woesei alpha-amylase [Pyrococcus woesei],1MXD_A Structure of a (Ca,Zn)-dependent alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei [Pyrococcus woesei],1MXG_A Crystal Structure of a (Ca,Zn)-dependent alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei in complex with acarbose [Pyrococcus woesei]
3QGV_A	2.73e-106	44	466	11	430	Crystalstructure of a thermostable amylase variant [Pyrococcus woesei]
4UZU_A	3.76e-44	42	465	5	478	Three-dimensionalstructure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolution [Geobacillus stearothermophilus]
1HVX_A	1.02e-43	42	465	5	480	BACILLUSSTEAROTHERMOPHILUS ALPHA-AMYLASE [Geobacillus stearothermophilus]
6AG0_A	7.22e-42	42	465	32	507	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P06279	9.29e-43	42	465	39	514	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
P26613	5.12e-41	42	467	3	491	Cytoplasmic alpha-amylase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amyA PE=3 SV=3
P26612	9.92e-41	42	467	3	491	Cytoplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=amyA PE=1 SV=3
P19571	1.24e-38	30	465	23	515	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
Q8VZ56	1.89e-38	44	412	27	404	Alpha-amylase 1 OS=Arabidopsis thaliana OX=3702 GN=AMY1 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
0.000000	0.000000	1.000055	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003119_00260.