CAZyme Information: MGYG000002157_01350

Basic Information

• Species: Amulumruptor sp001689515
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Amulumruptor; Amulumruptor sp001689515
• CAZyme ID: MGYG000002157_01350
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
933	MGYG000002157_23|CGC1	104287.99	6.0976

Genome Property

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

• Gene Location: Start: 15708; End: 18509 Strand: +

Full Sequence      

MKKHLYLLLLALFATIGAKAQLFTTSPTPLQNSSKDVVITFTADNSADGKKFANVTTDLY
AHIGVYTTVSPSQWKNAPAWGTNTAKYTFKYTSPKTWKLTIGDLRQYFNITDPNERITKV
CIIARNAAGSVQTADNFIDVMEDGFGALLTNDAEATVITAAKTINFTLSTTEAANLSIVI
SKDGTKVADKSQANATTLSLGYNFATKGAYTVTATANNGKETITKTTTILFMSASPAANY
PGGVPKMGPVAQSNGDVIFCLAAPQKSSVLLVPSWDDYQTLDKNVMSYQDYNGYRYFWIR
VSGLDPDKQYPYYFIVDGTISVGDPYAKLVLDCYSDKWLPDNVYPNRPRYPYDKLDNTML
AVYHGNQDKYNWKVKNFDTPDPSKLIIYEMLFRDFTGDGTDQDGKFFGTIRGAIDKFQYF
LDLGVNAIELMPIMEFNGNNSWGYNNNFYMALDKAYGSPDDLKEFIDLCHQHDIAVLLDI
VFNQSDGLHPWYQMYPIESNPFYNKTAPHNWSVLNDWKQENPLVQQQWKDVIAYWLTEYK
VDGFRFDLVKGLGVGATSGAYGSTDGYNAKRIENMKKIHKYVTDVNPKAIHINELLGDSK
EEVEYGKDGQYNWNNQNWLSGAFAAGLPNIAEKLNYFSTSACGRYGRSNISYAESHDEER
LGYMQINKNATWQKGTTTYKNQMVDTKGNPVALSDRMSRLGAVAIHLLMTKDATPMIWQF
GELGADQTTKEANGGNDTSPKKVIWNYYEDPSRKALFDTYSKMIHLRRANPELFSDNAAV
HSYSSNSTNLTGAYWVRIKNGTKDVIAFINADPKKENSVTLREDMTSDYRLVTSSKDFQP
SIPAGTGSRRITIPANGYAVFSSPSTSDIDNIYNDGFASDINIYGGEGCVIVEGAYDSLK
VYDLQGRAYRNSDLREGVYIVNVDGQTAKVMVR

Enzyme Prediction     

No EC number prediction in MGYG000002157_01350.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	407	731	1.3e-43	0.9464882943143813

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	2.39e-123	370	777	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	8.81e-45	364	549	12	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	7.60e-35	246	549	25	305	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
COG1523	PulA	7.01e-33	324	777	108	595	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	1.49e-31	386	725	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
QCD35300.1	1.32e-261	3	933	2	927
QIM10833.1	8.31e-241	15	933	2	908
QQR08212.1	4.31e-184	12	779	13	701
ANU64421.1	4.31e-184	12	779	13	701
ASB37479.1	4.31e-184	12	779	13	701

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3M07_A	5.17e-25	292	549	70	287	1.4Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium. [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
1EHA_A	8.41e-24	256	611	10	306	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
1EH9_A	1.48e-23	256	549	10	254	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGG_A	1.48e-23	256	549	10	254	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	4.62e-23	256	549	10	254	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q55088	8.18e-23	256	549	11	255	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
P14899	2.25e-22	358	614	19	268	Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC PE=3 SV=2
P95867	2.57e-22	312	549	43	257	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
B9G434	3.01e-22	353	776	218	682	Isoamylase 3, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=ISA3 PE=2 SV=1
Q9M0S5	1.84e-20	317	548	180	429	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
0.000245	0.999100	0.000174	0.000160	0.000154	0.000143

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002157_01350.