CAZyme Information: MGYG000003754_00082

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae; Porphyromonas
• CAZyme ID: MGYG000003754_00082
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
554		63175.76	5.4009

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003754	1700916	MAG	Canada	North America

• Gene Location: Start: 11700; End: 13364 Strand: -

Full Sequence      

MGKTMIYSYIPRLFRGVAAPLVAGGSYEQNGSGKFADMDEKALQQLRSMGFTHIWPIGVI
RHASRCAFPEQGIEADPQATVKGQAGSPYAIADYFDVAPYLAHDPAKRMEEFEALLERSH
RMGLKCIIDFVPNHVARTYHSLSHKDFGVADDRTKRYERDNNFYWLPDEKLILEGTPNYT
EFPARVTGNDRFTTQVGANDWYDTVKLNYGIDYTTTPPREDFEPIPATWHDMLEILLYWA
EKGVDGFRCDMAEMVPEAFWRWVIPIVKARYAVCFIAEIYRTELYEAFRLAGFDYLYDKV
GLYDTLIDVTKGFRPAEAIRGALEAEAGYREHMLTFLENHDEYRLASKGCLGSAKVAIPA
LAVALFAGKGPYMHYFGQALCEEASRPVGFSKGAGRTSIYDFVEVPSVSSWIRGDYTDFY
LGHKEKRLSERYKEMLYWTSALKVVEEGSYYYLPSESYKVEGADPSKLYLFLRYNEDEVL
LSASNFSTQEAHITLRWPSHLLDLMKIGDGERVARLVDLNGTKVLPYCSIASFAPLSFEV
NKQEVTLLHFILQE

Enzyme Prediction     

No EC number prediction in MGYG000003754_00082.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	30	385	3.7e-142	0.9946666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11349	AmyAc_3	0.0	4	436	1	447	Alpha amylase catalytic domain found in an uncharacterized protein 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; 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.
cd11313	AmyAc_arch_bac_AmyA	9.12e-47	40	434	25	329	Alpha amylase catalytic domain found in archaeal and 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, bacteroidetes, and proteobacteria. 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.
cd11347	AmyAc_1	3.74e-42	34	378	24	344	Alpha amylase catalytic domain found in an uncharacterized protein 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; 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	3.97e-20	6	380	2	258	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.
COG0366	AmyA	2.22e-19	6	495	3	492	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AOH39793.1	5.39e-151	3	519	7	532
AVV53664.1	5.39e-151	3	519	7	532
AHF12174.1	1.67e-147	3	511	5	524
QQR07864.1	3.42e-144	3	519	5	529
ASB37124.1	3.42e-144	3	519	5	529

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	6.02e-18	32	383	26	317	Crystalstructure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_B Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_C Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_D Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum]
4GKL_A	3.85e-15	40	346	28	262	Crystalstructure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana],4GKL_B Crystal structure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana]
6LGG_A	1.11e-13	89	258	97	247	Bombyxmori GH13 sucrose hydrolase mutant E322Q complexed with sucrose [Bombyx mori],6LGG_B Bombyx mori GH13 sucrose hydrolase mutant E322Q complexed with sucrose [Bombyx mori],6LGH_A Bombyx mori GH13 sucrose hydrolase mutant E322Q covalent intermediate [Bombyx mori],6LGH_B Bombyx mori GH13 sucrose hydrolase mutant E322Q covalent intermediate [Bombyx mori],6LGI_A Bombyx mori GH13 sucrose hydrolase mutant E322Q covalent intermediate complexed with fructose [Bombyx mori],6LGI_B Bombyx mori GH13 sucrose hydrolase mutant E322Q covalent intermediate complexed with fructose [Bombyx mori]
6LGA_A	1.11e-13	89	258	97	247	Bombyxmori GH13 sucrose hydrolase [Bombyx mori],6LGA_B Bombyx mori GH13 sucrose hydrolase [Bombyx mori],6LGB_A Bombyx mori GH13 sucrose hydrolase complexed with glucose [Bombyx mori],6LGB_B Bombyx mori GH13 sucrose hydrolase complexed with glucose [Bombyx mori],6LGC_A Bombyx mori GH13 sucrose hydrolase complexed with 1-deoxynojirimycin [Bombyx mori],6LGC_B Bombyx mori GH13 sucrose hydrolase complexed with 1-deoxynojirimycin [Bombyx mori],6LGD_A Bombyx mori GH13 sucrose hydrolase complexed with 1,4-dideoxy-1,4-imino-D-arabinitol [Bombyx mori],6LGD_B Bombyx mori GH13 sucrose hydrolase complexed with 1,4-dideoxy-1,4-imino-D-arabinitol [Bombyx mori],6LGE_A Bombyx mori GH13 sucrose hydrolase complexed with acarbose [Bombyx mori],6LGE_B Bombyx mori GH13 sucrose hydrolase complexed with acarbose [Bombyx mori]
6LGF_A	4.48e-13	89	258	97	247	Bombyxmori GH13 sucrose hydrolase mutant D247N complexed with sucrose [Bombyx mori],6LGF_B Bombyx mori GH13 sucrose hydrolase mutant D247N complexed with sucrose [Bombyx mori]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
L8B068	4.57e-16	89	386	300	544	Alpha-amylase MalA OS=Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1) OX=1227453 GN=malA PE=1 SV=1
Q2RTZ1	5.15e-13	33	297	255	469	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1) OX=269796 GN=glgE PE=3 SV=1
O16098	1.47e-12	89	257	140	287	Maltase 1 OS=Drosophila virilis OX=7244 GN=Mal-B1 PE=3 SV=2
Q9JN46	1.61e-10	20	310	201	446	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase (Fragment) OS=Cereibacter sphaeroides OX=1063 GN=glgE PE=3 SV=2
Q91WV7	3.09e-10	89	258	174	321	Neutral and basic amino acid transport protein rBAT OS=Mus musculus OX=10090 GN=Slc3a1 PE=1 SV=1

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
1.000055	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003754_00082.