CAZyme Information: MGYG000001910_02353

Basic Information

• Species: Duncaniella dubosii
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Duncaniella; Duncaniella dubosii
• CAZyme ID: MGYG000001910_02353
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
850	MGYG000001910_40|CGC1	93048.84	4.583

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001910	3154435	MAG	Denmark	Europe

• Gene Location: Start: 6856; End: 9408 Strand: -

Full Sequence      

MRLNLRHLWAMSAISASVAVSAQSITTSPAIITEDSKDIVITFHSDGGNRGLVDASASTG
IYAHTGVITNLSDGQWKNAPTWGTNTEKYKLTYTGPFTWEMRIPDLREYYNITASNENIE
KLAFVFRNSDGSSECKTGCGGDIFVQVFPKNFPASKEAVYPGGTPKMGTEINADGSVTFC
IAAPGKTNAVMMGSWNDYTAAPEYVMNYQDYNGNRYFWLTLDNLEKGKDYIYYYNIDGSI
NVGDPYARLVLDPNNDQYISSSVFPGLPAYPSKKITGVPLAIFNSERDVYDWKVTDFKGV
PQSDLIIYELLIRDFTGTEGKALGEGTVKGVISKLDYLKELGVNAIELLPIMEFAGNNSW
GYNTNFYMAPDKAYGTPDDYRALIDGAHERGMAVILDIVFNQSDGAHPWFDMVRRNISPF
YNGSAPHAYSVLNDWNQDCELVQQQWRDALDYWMTAYKVDGFRFDLVKGLGDNDSYGNTF
DAATNTWGTPNDNNTNRFNATRVARMKALHESMMLTNPDAYFINENLAGSEEENDMARDG
EINWANVNWSARNYVMGTGDTSLSRFYAPQDGNRLWGSTVSYAESHDEERVAYGTTSGTS
VVKGDFTALCQRIGSMAAQMLLSPGAHMIWQFEEIANNQTTKNNSGNDTSPKKVTWDISS
SPARQGLLATFKALCGIRADYPALFRENATAGVELSSTTARYISLTDGTSELYLVVNPAS
AKVTESATIPFPTNPATGTTAFLSDNKYSLVAASADVTPSMTANGITLPAGAFAVYVSGP
KSGITDIITNGEATSRPVVVTDGGHIRVLSPYTSFSIYTLGGMSLPTESRLEPGIYIVVV
DSNAVKVAVM

Enzyme Prediction     

No EC number prediction in MGYG000001910_02353.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	325	642	8.3e-47	0.9431438127090301

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	2.12e-118	290	688	1	390	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	6.50e-51	290	467	23	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	3.44e-40	166	474	25	312	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
COG1523	PulA	4.23e-37	244	688	108	595	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	2.35e-36	306	637	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
QCD42371.1	0.0	167	850	1	684
QCD35300.1	4.17e-307	19	849	18	926
QQR08212.1	7.40e-278	22	722	26	734
ANU64421.1	7.40e-278	22	722	26	734
ASB37479.1	7.40e-278	22	722	26	734

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3M07_A	8.87e-30	212	472	70	292	1.4Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
1EH9_A	4.25e-28	216	472	42	259	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGG_A	4.25e-28	216	472	42	259	Crystalstructure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltoheptaose [Saccharolobus solfataricus],3VGH_A Crystal structure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]
1EHA_A	4.25e-28	216	472	42	259	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGD_A	1.34e-27	216	472	42	259	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P95867	9.93e-30	216	473	43	263	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q55088	2.34e-27	216	472	43	260	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
O04196	1.05e-25	228	490	139	442	Isoamylase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=ISA1 PE=1 SV=1
O22637	9.86e-25	233	490	170	449	Isoamylase SU1, chloroplastic OS=Zea mays OX=4577 GN=SU1 PE=1 SV=1
Q9M0S5	4.97e-24	234	470	177	433	Isoamylase 3, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=ISA3 PE=1 SV=2

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
0.000761	0.998415	0.000204	0.000246	0.000188	0.000170

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001910_02353.