CAZyme Information: MGYG000000354_00942

Basic Information

• Species: CAG-485 sp001701295
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp001701295
• CAZyme ID: MGYG000000354_00942
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
569		65241.87	4.8184

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000354	2905675	MAG	Sweden	Europe

• Gene Location: Start: 50667; End: 52376 Strand: -

Full Sequence      

MKKKLIIYQAFPRIFTNMNADCVPGGTYEENGSGKLDDISPRLLKSLSDMGVNCIWLTGI
IEMATKTAFADGKIPADNPNVVKGQAGSPYAIKDYYDVSPAIATDVDRRMEEFEAVVKRT
HEAGMSIIIDFMPNHTARVYHSDSAPTGIRDFGSDDDFSKFFARDNNYYYITNQRFAPSF
DIARPGTEPYVEFPAKATGNDCFTAFCSETDWYETVKLNYGFDPGDWSTHYDPVPDTWLK
MLHILRFWASKGIDGFRCDMVFMVPREFWHWAIPQVKADYPDIIFIGEIYEVDAYSPFIE
YCHFDYLYDKVNLYDTLKGIECNNLSAAQLSSCWQRIDGIGDSMLNFLENHDEVRFASRE
FADNPAKVVPYLVVSAMISKGPFMIYYGQELGEMAHDNEGFAGDNNRSTIFDYWSYDTLR
RWYDNGKCSVRHLTPHEKWLRAVYSRILNLCNDIAAIREGNFFDLMYVNLRNPKFDPHRQ
FAFIRYTDSEILLFVVNFDSKPANVGVIIPDLAFDMAIIEEGIFHETDLIWGLDHTLDVR
RGQPVNMEIGGYDALIVPLKKIVAKTSHK

Enzyme Prediction     

No EC number prediction in MGYG000000354_00942.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	31	396	2.1e-156	0.9946666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11349	AmyAc_3	0.0	5	457	1	456	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	2.00e-49	1	460	1	336	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	7.72e-30	35	392	24	347	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.
pfam00128	Alpha-amylase	4.66e-25	34	392	1	327	Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.
COG0366	AmyA	8.67e-24	6	499	2	484	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCD40429.1	5.17e-253	1	556	6	560
QCP71534.1	5.17e-253	1	556	6	560
QCD41202.1	1.18e-248	1	556	2	556
QCD35086.1	2.06e-242	2	560	3	560
QQR07864.1	2.29e-231	3	560	4	560

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	3.59e-18	44	390	36	313	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]
1WZA_A	7.83e-18	8	507	8	448	Crystalstructure of alpha-amylase from H.orenii [Halothermothrix orenii]
4GKL_A	1.71e-17	3	390	4	291	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]
6Y9T_A	1.66e-15	6	392	29	392	FamilyGH13_31 enzyme [Lactobacillus acidophilus NCFM],6Y9T_B Family GH13_31 enzyme [Lactobacillus acidophilus NCFM]
4AEE_A	1.89e-14	47	505	274	653	CrystalStructure Of Maltogenic Amylase From S.Marinus [Staphylothermus marinus],4AEE_B Crystal Structure Of Maltogenic Amylase From S.Marinus [Staphylothermus marinus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q17058	6.44e-14	1	501	26	511	Alpha-glucosidase OS=Apis mellifera OX=7460 PE=1 SV=1
L8B068	7.53e-14	6	506	249	620	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
Q59226	2.57e-13	3	499	129	535	Cyclomaltodextrinase OS=Bacillus sp. OX=1409 GN=CDI5 PE=1 SV=1
P21332	1.83e-12	3	560	7	558	Oligo-1,6-glucosidase OS=Bacillus cereus OX=1396 GN=malL PE=1 SV=1
B3DYJ8	4.95e-12	8	290	212	423	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Methylacidiphilum infernorum (isolate V4) OX=481448 GN=glgE PE=3 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
1.000073	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000354_00942.