CAZyme Information: MGYG000004758_01092

Basic Information

• Species: Prevotella sp900553155
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900553155
• CAZyme ID: MGYG000004758_01092
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
711	MGYG000004758_33|CGC1	81234.03	6.3307

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004758	2740450	MAG	Denmark	Europe

• Gene Location: Start: 18329; End: 20464 Strand: +

Full Sequence      

MGNQKIIIYQIFTRLFGNRTNVCKHNGTIAENGCGKMNFFTDEVLQQIRAKGYTHVWYTG
VIRHATATDYSPYGIPRQHPAIVKGKAGSPYAITDYYDIDPDIAENVDKRMDEFLKLVDN
SHRNGLEVIMDFVPNHVARQYKSIAKGKGVRDLGEDDDKTKAFDANNNFYYCVNSAFAPS
IDLYSGEAEPYSEFPAKATGNDQFGASPSCNDWYETVKLNYGVDYCDSGGRSEHFDPIPN
TWHKMLDILLYWASKGVDGFRCDMAEMVSTAFWHWAIDKVKSVHPAMIFIAEVYNPWEYK
HYVDAGFDYLYDKVGMYDTMRGVICGNCPTSQITIAWQWVDGISNHMLYFLENHDEQRIA
SDYFAGDGFRAYPALAVNMLMRSNPFMVYAGQEYGERGMDSEGFSGKDGRTTIFDYWTIP
SLHRALVTNESTASERKLSAIYDRILSIASTEKAVAEGQFFDLMYVNEHIAQRQYAFLRK
AGDEMLLVVANFANEAVSVRINIPEHAFSFLGIPKSDITGKDMVRLSSFKANFKTDNFVD
VEIGANDCKIIKFNLKMDIDITFNEHNKEEFPPAHTAEHLLNQTMVRMFCCKRSDNAHIE
RKKSKITFIIDHKPSRKEEKAIEDRMNELINADLPVRYEVVDRDKLPKEVDANRLPADVS
SKVRLVYIGDYDVCPCIGKHVRSTSQIGRFVMLGTNWDEIKHAFRIRFKIV

Enzyme Prediction     

No EC number prediction in MGYG000004758_01092.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	32	400	6.9e-168	0.9973333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11349	AmyAc_3	0.0	6	455	1	456	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 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	2.26e-47	7	458	6	336	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.
cd11347	AmyAc_1	5.27e-40	7	397	2	349	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 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.
COG0366	AmyA	2.78e-30	7	501	2	492	Glycosidase [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	8.34e-22	7	381	1	241	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
QKH87711.1	0.0	5	711	4	719
QUB77127.1	0.0	5	711	4	719
QUB72719.1	0.0	5	711	4	719
QUB39972.1	0.0	5	711	4	719
QUB85710.1	0.0	5	711	4	719

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4GKL_A	3.41e-18	1	527	1	400	Crystalstructure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana],4GKL_B Crystal structure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana]
7JJT_A	1.44e-17	82	501	82	480	ChainA, Alpha-amylase [Ruminococcus bromii]
1WZA_A	8.59e-16	82	501	57	448	Crystalstructure of alpha-amylase from H.orenii [Halothermothrix orenii]
1JF5_A	3.53e-15	91	505	204	547	ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF5_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]
1WZK_A	4.67e-15	91	505	204	547	ChainA, Alpha-amylase II [Thermoactinomyces vulgaris],1WZK_B Chain B, Alpha-amylase II [Thermoactinomyces vulgaris]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q08751	2.56e-14	91	505	204	547	Neopullulanase 2 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaII PE=1 SV=1
P20845	1.09e-12	91	501	101	488	Alpha-amylase OS=Priestia megaterium OX=1404 PE=1 SV=1
P14899	1.36e-12	91	530	88	480	Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC PE=3 SV=2
Q59226	2.84e-09	82	491	194	533	Cyclomaltodextrinase OS=Bacillus sp. OX=1409 GN=CDI5 PE=1 SV=1
P14898	4.97e-09	1	502	129	531	Alpha-amylase 2 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyB PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000026	0.000014	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004758_01092.