CAZyme Information: MGYG000002841_02334

Basic Information

• Species: UBA5446 sp900544765
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UBA5446; UBA5446 sp900544765
• CAZyme ID: MGYG000002841_02334
• CAZy Family: CBM34
• CAZyme Description: Neopullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
570	MGYG000002841_15|CGC2	65004.66	6.1648

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002841	2563577	MAG	Germany	Europe

• Gene Location: Start: 48524; End: 50236 Strand: +

Full Sequence      

MNFAAIEHRPVSEYCHGLDEGRIVYRLRCARGDLERVTLSYGDTACRVTPIIFTPVEMEL
AASDEYHDYWQAVVESKYYRVYYYFTLYGGGEWTYYYGGEFTKSLVDDRSEYFKLPINHR
ADIARVPDWARDAVVYNIFPDSFASGEGSIPGSGAELFHNGQRVRGRLGGTLDGVAANAK
YIRSMGFSCVYLNPIFAAGEYHKYDTIDYMHVDPCFGGDGAMRRMVKALHAEGIRVIIDG
VFNHCGWRFWAFEDVIKNQERSRYRDWFYGLTFPVERPADPEAYPGYTTYAYERMMPKLN
TANREVREYLCGVGQYWIEEFGVDGWRLDVASEVDDGFWRAFRAAVKAVKPDALLIGEVW
ETARHWLDGDMFDSTMNYDFRKHCRRFFAEGSLDAYGFAARCSDMLMRYKLQMTGVQMNL
LDSHDVSRFLSVCGGDKRRYRLALLFLMCFVGMPMLFYGDELGMEGVAELDYRSPMPWGS
GDTHLRDFVRRAIALRHERTELRRGSFRVISAQPGSGLLAFERRYGGKALAVCLNAGGTP
APAPASGETLWADGLENGVLAPWGFAVFEK

Enzyme Prediction     

No EC number prediction in MGYG000002841_02334.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	170	467	7.2e-121	0.9866666666666667
CBM34	7	122	7e-19	0.975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	0.0	132	507	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	2.93e-97	8	538	7	560	maltodextrin glucosidase; Provisional
cd11353	AmyAc_euk_bac_CMD_like	6.28e-73	132	507	1	366	Alpha amylase catalytic domain found in eukaryotic and bacterial 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.
pfam00128	Alpha-amylase	7.46e-68	170	467	1	331	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	5.21e-63	181	507	36	328	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
QNM01432.1	1.51e-232	1	569	1	578
QNO17836.1	1.19e-207	1	570	1	572
QUH29228.1	4.94e-203	1	570	1	576
BCJ94875.1	5.13e-192	1	537	1	546
BCN31338.1	3.39e-185	1	568	1	578

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1J0H_A	6.81e-137	1	568	1	583	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]
1J0J_A	1.92e-136	1	568	1	583	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]
1SMA_A	1.53e-135	1	568	1	583	CrystalStructure Of A Maltogenic Amylase [Thermus sp. IM6501],1SMA_B Crystal Structure Of A Maltogenic Amylase [Thermus sp. IM6501]
1GVI_A	2.42e-134	1	568	1	583	Thermusmaltogenic amylase in complex with beta-CD [Thermus sp.],1GVI_B Thermus maltogenic amylase in complex with beta-CD [Thermus sp.]
1JF6_A	6.97e-133	1	555	1	557	ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF6_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P38940	2.10e-135	1	568	1	583	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
A0A7U9P668	2.96e-135	1	568	1	583	Cyclomaltodextrinase OS=Geobacillus thermopakistaniensis (strain MAS1) OX=1408282 GN=T260_08735 PE=1 SV=1
Q08751	1.52e-131	1	555	1	557	Neopullulanase 2 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaII PE=1 SV=1
Q08341	1.37e-121	5	535	6	535	Cyclomaltodextrinase OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1
P29964	2.89e-119	5	535	5	531	Cyclomaltodextrinase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=Teth39_0676 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
1.000076	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002841_02334.