CAZyme Information: MGYG000000353_01424

Basic Information

• Species: UBA7173 sp900548705
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173; UBA7173 sp900548705
• CAZyme ID: MGYG000000353_01424
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
598	MGYG000000353_12|CGC1	67580.26	6.328

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000353	2738445	MAG	Sweden	Europe

• Gene Location: Start: 11114; End: 12910 Strand: +

Full Sequence      

MAKEKTTVKKAPAKAGKTIETKGLENTLIQNRRPVIYQMFPRLFSNTTADCIPDGDISRN
GCGKMNDITPKVFKAISGLGITHVWYTGVIEHAHATDYSAYGITPDNPYVVKGKAGSPYA
ISDYYDIDPDIAVSVPERMKEFEALVERTHAAGMKVLIDFVPNHVARRYHSDVAPAGIED
FGQGDDPTYFFSPRNNFYYIPRQLFQPGFDIGDYTEFPSKASGNDCFNAFPSRNDWYETV
KLNYGVDYGDGSRHFDPVPPTWFKMLHILRYWASKGVDGFRCDMVFMVPVEFWEWAIPQV
KAHYPDITFIAEIYDVGQYREFLERGHFDYLYDKVNLYDTLRAVQCYHHSAATITDCWQR
VDGIGGKMLNFLENHDEQRFASEQYAGDAAKVLPSLVVSSMISTGPFMLYAGQELGEKAE
DAEGFSGKDGRTTIFDYWSVPTLRRWFNNGKADGGQLSTVEKDLRGVYAHVLGLLNSEKA
LAEGEFFDLMYVNFNNPDFNPHRHYAFLRRHGDDVILIAVNFSDVAAQLAINIPALALGM
YGIKEGTKKGKELISGREADLTVSRDEPFTTHIAPWGAVAWKFSASRNRRKNICRSKE

Enzyme Prediction     

No EC number prediction in MGYG000000353_01424.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	60	421	1.6e-170	0.9973333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11349	AmyAc_3	0.0	34	481	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	5.05e-47	32	484	3	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	4.84e-36	64	418	24	349	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.
COG0366	AmyA	2.88e-28	35	536	2	495	Glycosidase [Carbohydrate transport and metabolism].
pfam00128	Alpha-amylase	1.25e-21	63	416	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCD40429.1	4.38e-276	29	591	5	571
QCP71534.1	4.38e-276	29	591	5	571
QCD35086.1	8.32e-276	29	593	1	564
QCD41202.1	2.13e-273	29	590	1	566
QQR07864.1	9.12e-270	31	593	3	564

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	1.21e-21	23	414	2	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]
4GKL_A	7.96e-16	71	381	29	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]
6AAV_A	9.88e-16	32	539	14	523	Crystalstructure of alpha-glucosyl transfer enzyme, XgtA at 1.72 angstrom resolution [Xanthomonas campestris],6AAV_B Crystal structure of alpha-glucosyl transfer enzyme, XgtA at 1.72 angstrom resolution [Xanthomonas campestris]
1WZA_A	2.46e-14	37	460	8	390	Crystalstructure of alpha-amylase from H.orenii [Halothermothrix orenii]
3WY1_A	3.76e-14	24	433	1	405	Crystalstructure of alpha-glucosidase [Halomonas sp. H11],3WY1_B Crystal structure of alpha-glucosidase [Halomonas sp. H11],3WY2_A Crystal structure of alpha-glucosidase in complex with glucose [Halomonas sp. H11],3WY2_B Crystal structure of alpha-glucosidase in complex with glucose [Halomonas sp. H11]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9Z3R8	1.02e-15	32	536	19	521	Probable alpha-glucosidase OS=Rhizobium meliloti (strain 1021) OX=266834 GN=aglA PE=3 SV=2
P14899	4.71e-15	32	485	33	426	Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC PE=3 SV=2
O16098	3.23e-13	32	288	84	285	Maltase 1 OS=Drosophila virilis OX=7244 GN=Mal-B1 PE=3 SV=2
L8B068	7.77e-13	35	566	249	649	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
P38940	9.22e-13	35	581	136	583	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT 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
1.000046	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000353_01424.