CAZyme Information: MGYG000002872_00946

Basic Information

• Species: UMGS874 sp900546315
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; UMGS874; UMGS874 sp900546315
• CAZyme ID: MGYG000002872_00946
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
652	MGYG000002872_21|CGC1	72980.02	4.5534

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002872	3007809	MAG	United States	North America

• Gene Location: Start: 20981; End: 22939 Strand: +

Full Sequence      

MNAFSDIDALIRCGARVSLSLARRDGGSVGFMGRDAYPFGTVLDFTVCVPRAFSVDSVVM
RLYRDDDMSRRELPLTLSGFGDSADIYSCPVDTGEICLDGSGLFYYDFELTTPLGKVRTN
QDGSVTDGSPDSRQLLVYPKDYTVPERFAGGMMYQIFPDRFATGGKRYTSREELTFIGGQ
KRIINPDWETGVPEYAGKPGDELDNNEFFGGSIQGIIDNFDYIKSLGVRTIYLNPIFEAA
SNHRYDTGDYMKIDPLLGDTDAFEELCAKAKEKDMLVILDGVFGHTGADSVYFNRFGNYP
GKGAYQSESSDYSEWYDFRRWPDDYRCWWGVKILPQTRTADESFVGFICGKDDTDGVVGN
WLNHGAGGWRLDVADELSDKLLSEIRKSAKRADPEAIIIGEVWEDASNKVAYSERRKYFR
GGQLDSVMNYPLKDGVTDYVMSGDKTRLYEVLTTIYPHYPEMVGHVLMNFLGTHDTERIL
TVLAGVGAERMTNAELAVYRLPDDKRELAENRLRLAWAILCALPGMPCVYYGDERGMEGG
RDPFNRMPFVRSETPLTDFYREAGRVRNGNPALLHGDISLPETGDMSQILIVRRYNSDVT
AVAANMSDRPWDIETGRGGEVLLSACVENTARVVISDNYVTIPPRSVVYIGL

Enzyme Prediction     

No EC number prediction in MGYG000002872_00946.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	211	543	1e-119	0.9936708860759493

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	9.25e-166	150	578	1	389	Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). 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.
PRK10785	PRK10785	1.21e-81	154	608	125	560	maltodextrin glucosidase; Provisional
PRK14510	PRK14510	5.96e-65	38	612	15	607	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
pfam00128	Alpha-amylase	1.25e-51	211	543	1	334	Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.
cd11337	AmyAc_CMD_like	1.32e-51	213	577	27	327	Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is mainly bacterial. 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
QNK39367.1	4.90e-150	32	607	8	574
QAT48387.1	7.60e-148	36	605	15	572
BCI61467.1	8.85e-147	36	627	19	596
CAB1239245.1	2.34e-143	40	579	19	547
QQR32000.1	7.16e-143	40	595	19	561

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1J0H_A	1.63e-60	142	613	126	544	Crystalstructure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0H_B Crystal structure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0I_A Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus],1J0I_B Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus]
5Z0U_A	3.29e-60	105	597	89	564	Thermoactinomycesvulgaris R-47 alpha-amylase I (TVA I) 11 residues (from A363 to N373) deletion mutant (Del11) [Thermoactinomyces vulgaris]
1J0J_A	4.32e-60	142	613	126	544	ChainA, neopullulanase [Geobacillus stearothermophilus],1J0J_B Chain B, neopullulanase [Geobacillus stearothermophilus],1J0K_A Chain A, neopullulanase [Geobacillus stearothermophilus],1J0K_B Chain B, neopullulanase [Geobacillus stearothermophilus]
5Z0T_A	7.27e-59	105	597	89	575	Thermoactinomycesvulgaris R-47 alpha-amylase I (TVA I) mutant A357V/Q359N/Y360E (AQY/VNE) [Thermoactinomyces vulgaris],5Z0T_B Thermoactinomyces vulgaris R-47 alpha-amylase I (TVA I) mutant A357V/Q359N/Y360E (AQY/VNE) [Thermoactinomyces vulgaris]
1SMA_A	8.00e-59	142	613	126	544	CrystalStructure Of A Maltogenic Amylase [Thermus sp. IM6501],1SMA_B Crystal Structure Of A Maltogenic Amylase [Thermus sp. IM6501]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P36905	1.23e-90	55	578	289	832	Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P38536	1.97e-89	38	578	268	831	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P38939	3.67e-89	96	586	337	840	Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P16950	6.93e-87	96	586	337	841	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
Q08341	2.68e-62	142	613	125	543	Cyclomaltodextrinase OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1

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
1.000069	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002872_00946.