CAZyme Information: MGYG000003831_00729

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485
• CAZyme ID: MGYG000003831_00729
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
935	MGYG000003831_15|CGC2	102191.7	4.9724

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003831	3246644	MAG	United States	North America

• Gene Location: Start: 29728; End: 32535 Strand: -

Full Sequence      

MLKIYLLSLMAIVCSVFGVSAQIVTTEPSPLQEDSQNVVIYFHADQGNKGLINQPASAAL
YAHTGVSIVDAAGKAADWQHVPAEWNTNLPKCKLEYVSTNLWKLNIGDIRTFYGVPANEK
ITKLCFVFRSADGKKECKTATGGDIFVDVVDKGFQMSLTSSVPEGIVNASTGAVTFTMST
TQAASLSITVNDKELKTASGATSLSASYTFPAEGDYIVTATASAGPGNEIKYQTLSYCYA
GNSKPASGTALPRMGATRNSDGSITFCIAAPQKQSAMVVGSWNGYKYTNSQLMNYVDAQV
DGATFRHFTLTLPREATVGKGTLSYFYVVDGSIKVGDPYAELVLDPYNDKYISPEVFPNL
PEYPSDKLSGVPLAVLKEGLTDYTWQTKSFQAPAKTDLIIYEMLLRDFTGTEGKADGNGT
VRQAIAKIPYLKSLGINAVELLPINEFNGNISWGYNPNFYFAVDKAYGTPQDYKEFIDRC
HAEGIAVILDMVFNQSDGLHPWYMMYTPGENPFYNLNAPHAYSVLNDWNQGYPLVEQQWK
DVLQYWLKEYKVDGFRFDLVKGLGNNDSYANSGENATNAFNQSRIDRMKRLHSYMKEVNP
DAYFINENLAGAQEENQMAADGELNWANVNEAGGQFAMGYSEKSNLNRMLATQDGRTAGS
TVSYLESHDEQRLAYKQDIWGETGVKGNATVSCQRLGAAAAQMILVPGSHMIWQFSEMGN
SQNTKDANGGNNTDPKIVNWNLLNDPDHKGLFESYQQLIALRLGNKELFTPARGVDFSMQ
CNVSNWASGRTLTARTSDMELYCAINPNITGSLNIPVTFRTVDDNAYEIYSQSHGCQGSF
SATAGTITVPANCYVVVCSRNVSGVEEIENGITDSMRVSAGKGYISVDGATSPVEIIDIS
GRMITREESASFSVSLPSGIYIVKSGAKASKHMVR

Enzyme Prediction     

No EC number prediction in MGYG000003831_00729.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	418	726	6.4e-48	0.9464882943143813

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	2.43e-138	383	771	1	389	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	4.84e-46	381	560	21	190	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	3.66e-44	253	719	25	471	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
COG1523	PulA	2.44e-37	294	762	47	585	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	6.03e-37	399	720	1	259	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIM10833.1	0.0	24	935	10	908
QCD35300.1	9.23e-295	1	935	1	927
QQR08212.1	1.65e-240	21	834	26	757
ANU64421.1	1.65e-240	21	834	26	757
ASB37479.1	1.65e-240	21	834	26	757

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3M07_A	2.81e-24	383	560	122	287	1.4Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
1EHA_A	1.12e-23	325	563	42	257	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGG_A	1.12e-23	325	563	42	257	Crystalstructure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltoheptaose [Saccharolobus solfataricus],3VGH_A Crystal structure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]
1EH9_A	1.12e-23	325	563	42	257	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGD_A	3.49e-23	325	563	42	257	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q44316	1.10e-24	383	563	102	272	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter sp. (strain Q36) OX=104027 GN=treZ PE=3 SV=1
Q8CZE8	5.43e-24	266	769	39	518	1,4-alpha-glucan branching enzyme GlgB OS=Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831) OX=221109 GN=glgB PE=3 SV=1
Q9AJN6	2.18e-23	383	563	85	255	Malto-oligosyltrehalose trehalohydrolase OS=Arthrobacter ramosus OX=1672 GN=treZ PE=3 SV=1
Q55088	6.18e-23	325	563	43	258	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
P95867	6.25e-23	325	566	43	263	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000385	0.998873	0.000212	0.000171	0.000165	0.000151

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003831_00729.