CAZyme Information: MGYG000002157_02060

Basic Information

• Species: Amulumruptor sp001689515
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Amulumruptor; Amulumruptor sp001689515
• CAZyme ID: MGYG000002157_02060
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
928	MGYG000002157_57|CGC1	101987.82	4.9382

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002157	2499032	MAG	Germany	Europe

• Gene Location: Start: 730; End: 3516 Strand: +

Full Sequence      

MRHIYSSVVMWMTLGLPLAASAQVVTTSPAIVQTDSKNIVITFHADQGNKGLMGATSSTK
VYAHTGVITDKSDGQWAYAPTWLDNAAKYQLKYIAANTWTLSIPDITTYYGIKSGEAVEK
LAFVFRDATGSKEGKTASGGDIFVDVLPPGFQMVLESDLDGGMLTDNTPVKFTVNTTGNA
DISLYVNSENSTPIASGTATDQLQTSYSFTSPGDYTIIAVAKSGNVTRRQTLQVARLNAT
LSENYPGGVPKMGAVTNADGSVTFCLAAPKKSSAVIVGSWNDYTVSARNQMYRQDYQGNT
YFWTTVSGLKPATDYIYYYIIDGGISVGDPYARLVLDPWNDKYISASIFPNLPAYPEDKV
QNVPLAVYNSTRDAYDWKIKNFKGVDQSDLIIYELLIRDFTGTEGKAEGNGTLRGVIDKL
DYINGLGVNAVELLPIMEFNGNNSWGYNTNFYFAPDKAYGTPDDYRLLVDECHRRGMAVI
LDIVFNQSDGLHPWYQMYPIAQNPFYNGTAPHGYSVLNDWNQDNPLVQQQWHDALAYWME
AYNVDGLRFDLVKGLGNNTSYGATYNAATNTWSGVTDAKTNAYNATRVARMKTLHDAMRK
VKPDAYFINENLATPKEENEMAQDGEINWANINTESCQFAMGFSSNSNLRRFYAPDDSRT
WGSTVSYAESHDEERMAYKQTQYGANGVKGNIPMSMRRLGSVAAQMLMAPGAHMIWQFQE
FGADQTTKNANGGNNTDPKKVIWSYLDNPDRAGLAQNYRELNAIRTNNPQLFKQGVSTTM
QCSANNWANGRYIALTDGTAELYCVINPNISGSRAISVPMKQDASKYQILSKSYNVEPQI
GNKSITLPAGAYVVIGTKDLADRDEIMSDGTGSNVNVYGGEGCIIIDGAYDHADVYDISG
SRTDRTESLAPGIYVVVVDGNTSKVAVR

Enzyme Prediction     

No EC number prediction in MGYG000002157_02060.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	410	729	2.3e-48	0.9464882943143813

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	1.48e-131	375	772	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	3.55e-54	373	725	21	363	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	5.46e-42	251	723	25	472	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
cd11316	AmyAc_bac2_AmyA	2.81e-36	391	773	2	402	Alpha amylase catalytic domain found in 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 Chloroflexi, Dictyoglomi, and Fusobacteria. 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	1.28e-35	389	771	4	333	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
QCD35300.1	0.0	1	928	1	927
QIM10833.1	0.0	25	928	10	908
QQR08212.1	1.89e-308	16	835	20	758
ANU64421.1	1.89e-308	16	835	20	758
ASB37479.1	1.89e-308	16	835	20	758

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4J7R_A	2.36e-28	333	553	157	420	CrystalStructure of Chlamydomonas reinhardtii Isoamylase 1 (ISA1) [Chlamydomonas reinhardtii],4J7R_B Crystal Structure of Chlamydomonas reinhardtii Isoamylase 1 (ISA1) [Chlamydomonas reinhardtii],4OKD_A Crystal Structure of Chlamydomonas reinhardtii Isoamylase 1 (ISA1) in complex with maltoheptaose [Chlamydomonas reinhardtii],4OKD_B Crystal Structure of Chlamydomonas reinhardtii Isoamylase 1 (ISA1) in complex with maltoheptaose [Chlamydomonas reinhardtii]
3M07_A	1.78e-27	256	552	22	287	1.4Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
3VGG_A	1.57e-26	275	555	11	257	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	1.57e-26	275	555	11	257	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
1EH9_A	1.57e-26	275	555	11	257	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O04196	6.01e-27	314	551	140	411	Isoamylase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=ISA1 PE=1 SV=1
Q55088	8.64e-26	275	555	12	258	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
P95867	2.07e-25	375	559	90	264	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
B9G434	5.11e-25	219	553	72	448	Isoamylase 3, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=ISA3 PE=2 SV=1
O22637	3.61e-24	332	553	174	420	Isoamylase SU1, chloroplastic OS=Zea mays OX=4577 GN=SU1 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
0.000291	0.999032	0.000170	0.000182	0.000162	0.000148

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002157_02060.