CAZyme Information: MGYG000002878_00651

Basic Information

• Species: RC9 sp900546395
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9; RC9 sp900546395
• CAZyme ID: MGYG000002878_00651
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
972	MGYG000002878_14|CGC1	109271.39	4.4975

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002878	2590775	MAG	United States	North America

• Gene Location: Start: 18565; End: 21483 Strand: -

Full Sequence      

MKKILYMLCTVLLVFSCTKGPTFLELSTETVVIPIEGGTRIISLNCDGDWTLGMSEGSSW
CVPSEMSGSGNTRFSVRAESNIGGKSRKATLTFSVSGLESRKLVVEQEGEDSSSSGGSDK
GDFYPVPESGITLDPVKPNADQPCTIKFNPEPSNPLYNHKGELYGHLGVIVEDEWKFVPC
EWGVSDEKVHFTKTADNSWELKLEPSVREYFGSGTTPITKMAIIVRSEDGELKSHEADQF
CSVTDDLYQLEEFVPDPVVNETMPSGVQYGINCSPDGSVTFVFYDKNKFGERSEYCYIVG
DWNNWERVPEGAMKRDDAAGCWWITLDGFDQSEEYRYQYRLGKGSGADIRVDDPYTEIVY
DQWNDQYLSGIRPYPEGAKGLVSAFRISEDEYQWQHKDFRVEDKNDLIIYELLFRDFSVS
KDIAGAMAQMDYLEKLGVNAIELMPIQEFDGNLSWGYNPNHYFALDKAYGTREQYKEFID
ECHSRGMAVIVDVVYNHATGSHPWAKMYWNESKSCTSEQNPWFNVTATHPFSVFHDWNHE
NGMVREHVKRSLGYLLEEYDVDGFRFDLSKGFTQKNSGNDVGAWSAYDASRIAILRDYYD
YIQSVNSDAVVILEHLGDAKEERELAEFGAQLWRKVNNEYASALKGSRADFSAAYSASPF
GGYVSYMESHDEQRICYGATGASGSSDWGICGSFTGWGEKPDVKMVKDGSFYVSKSVDFP
QAAEFKVREGSVWDKGNYGAPGKTASLNAGESFALYSGPDSQNLRVDIAGKYDVYFSPST
AELWLMETGKRPSEPSVSEEDAPLALSMRRAGCCAAFFLTVPGPKMIWQFGELGYDISGG
NGDTSEKPVKTQEYLSDKYRKGLYDTYCGLLKFRRENPRFFDMDADFKWYVSNNEWDNGR
FIYCTADGKSFAVIGNFSTSDRNITAWLPVAGVWKDYEAFGSGTYNVTVDSEGHNSLSFN
LKPGEFRLIVKE

Enzyme Prediction     

No EC number prediction in MGYG000002878_00651.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	421	656	1.3e-42	0.6964856230031949

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	1.75e-148	392	881	1	387	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 (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.
cd11325	AmyAc_GTHase	8.52e-48	390	567	21	188	Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called Maltooligosyl trehalose Trehalohydrolase). Glycosyltrehalose trehalohydrolase (GTHase) was discovered as part of a coupled system for the production of trehalose from soluble starch. In the first half of the reaction, glycosyltrehalose synthase (GTSase), an intramolecular glycosyl transferase, converts the glycosidic bond between the last two glucose residues of amylose from an alpha-1,4 bond to an alpha-1,1 bond, making a non-reducing glycosyl trehaloside. In the second half of the reaction, GTHase cleaves the alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose and malto-oligosaccharide. Like isoamylase and other glycosidases that recognize branched oligosaccharides, GTHase contains an N-terminal extension and does not have the conserved calcium ion present in other alpha amylase family enzymes. 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. Glycosyltrehalose Trehalohydrolase Maltooligosyltrehalose Trehalohydrolase
COG0296	GlgB	3.32e-41	298	567	52	303	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd11341	AmyAc_Pullulanase_LD-like	1.59e-31	405	568	1	198	Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin endo-1,6-alpha glucosidase), limit dextrinase, and related proteins. Pullulanase is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. Pullulanases are very similar to limit dextrinases, although they differ in their action on glycogen and the rate of hydrolysis of limit dextrins. 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	6.25e-31	406	567	4	166	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADV44995.1	8.96e-229	6	954	14	851
SCD19325.1	1.35e-225	126	948	39	756
QCQ49667.1	4.28e-225	19	937	126	924
QCQ46983.1	3.39e-224	19	937	126	924
QLK84352.1	3.39e-224	19	937	126	924

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1EHA_A	1.28e-26	313	567	35	252	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
1EH9_A	1.28e-26	313	567	35	252	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGG_A	1.28e-26	313	567	35	252	Crystalstructure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltoheptaose [Saccharolobus solfataricus],3VGH_A Crystal structure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]
3VGD_A	4.01e-26	313	567	35	252	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]
3VGE_A	7.10e-26	313	565	35	250	Crystalstructure of glycosyltrehalose trehalohydrolase (D252S) [Saccharolobus solfataricus],3VGF_A Crystal structure of glycosyltrehalose trehalohydrolase (D252S) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q55088	7.04e-26	313	567	36	253	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
P95867	1.68e-25	313	567	36	255	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q44316	2.64e-23	312	567	39	267	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treZ PE=3 SV=1
Q53238	1.88e-22	306	567	34	265	Malto-oligosyltrehalose trehalohydrolase OS=Rhizobium sp. (strain M-11) OX=269089 GN=treZ PE=3 SV=1
Q9AJN6	4.75e-20	375	567	70	250	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter ramosus OX=1672 GN=treZ PE=3 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
0.000018	0.011689	0.988332	0.000004	0.000005	0.000004

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002878_00651.