CAZyme Information: MGYG000001795_02110

Basic Information

• Species: Amulumruptor caecigallinarius
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Amulumruptor; Amulumruptor caecigallinarius
• CAZyme ID: MGYG000001795_02110
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
924	MGYG000001795_19|CGC1	102367.39	4.9117

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001795	2604985	MAG	Denmark	Europe

• Gene Location: Start: 38459; End: 41233 Strand: +

Full Sequence      

MKKHLYLLLLALFATIGAKAELFTPSPYPLQNSSKDVVITFTADNSTDGKKFANITADLY
AHIGVYTTESPSTWKNAPAWGTNTSKYLFKYQGNKTWKLTIGDLRQYFNITDPNEIITKV
CIIARNSASNTQTADNFIDVLGDGFGAILNHDAEATVITAATDINFTLATTEAATLNIAI
TKDGSQVSSKDAANAKSLTLGYNFASKGAYVVTATANNGKETITKTINILYMSASPAATY
PGGVPKMGPVAQSNGDVIFCLAAPQKSSVLLVPSWDDYQTLDKNVMSYQDYNGYRYFWIK
VSGLDPDKQYPYYFIVDGNIKVGDPYAKLVLDCHSDKWLPDNVYPTRPRYPYDKMDGTML
AVYHGNQDNYNWKVQSFDIPDPSKLIIYEMLFRDFTGDGEDNSEEGKQLGTIRGAIDKFQ
YFLDLGVNAIELMPVMEFNGNNSWGYNTNFYMALDKAYGSPDDLKEFIDLCHQHDIAVLL
DIVFNQSDGLHPWYQMYSASANPFYNATAPHNWSVLNDWKQENPLVQQQWKDAIEYWMTK
YKVDGFRFDLVKGLGSGSTSSEYGSTDGYNAKRIANMKKIHTYITAVNPKGIHINEFLGD
TNEEIEYGQDGQYNWNNQNWLSAMYAIGQPGQAQRLGFYSSSACGRYGRSCISYAESHDE
ERLGYCQLTSTFNGTTNQMAKASLSDRMSRLGVVAVNLLMTKDATPMIWQFGELGADQTT
KDSSGGNDTSPKKVVWDYYDDPSRKALFDTYSKMIGIRRANPELFSDDAATFTYSSNSAN
ISGAYWVRIKNGAKDVIAFINASPTAAGNVTLRADMTSDYKLVTASEGFSPSIPAGTGTR
RITIPANGYAVFQSPSTADIDNIYNDGFASDINVYGGEGCVIVEGAYDSLRIYDLQGRSY
ANSDLSEGVYIVKVDGNTTKVMVR

Enzyme Prediction     

No EC number prediction in MGYG000001795_02110.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	409	722	2.9e-44	0.9464882943143813

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11350	AmyAc_4	5.99e-120	370	768	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	1.75e-43	370	718	23	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	3.11e-36	246	551	25	305	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
COG1523	PulA	6.27e-32	324	550	108	360	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	4.23e-31	386	716	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	1.45e-255	3	924	2	927
QIM10833.1	9.85e-240	15	924	2	908
QCD42371.1	1.35e-186	247	923	1	683
QQR08212.1	1.14e-181	12	770	13	701
ANU64421.1	1.14e-181	12	770	13	701

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1EH9_A	1.53e-25	254	554	8	257	CrystalStructure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGG_A	1.53e-25	254	554	8	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	1.53e-25	254	554	8	257	CRYSTALSTRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGD_A	4.80e-25	254	554	8	257	Ctystalstructure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]
3VGE_A	8.48e-25	254	554	8	257	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	8.44e-25	254	554	9	258	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
B9G434	5.62e-23	317	767	195	682	Isoamylase 3, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=ISA3 PE=2 SV=1
P95867	6.13e-23	312	554	43	260	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1
Q9M0S5	3.77e-22	317	771	180	669	Isoamylase 3, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=ISA3 PE=1 SV=2
O22637	3.59e-21	293	557	156	425	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
0.000232	0.999107	0.000177	0.000157	0.000152	0.000143

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001795_02110.