CAZyme Information: MGYG000004064_00394

Basic Information

• Species: UMGS755 sp900545185
• Lineage: Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UBA9506; UMGS755; UMGS755 sp900545185
• CAZyme ID: MGYG000004064_00394
• CAZy Family: GH13
• CAZyme Description: Amylopullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
614		69047.09	4.8866

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004064	2605118	MAG	United Kingdom	Europe

• Gene Location: Start: 55852; End: 57696 Strand: -

Full Sequence      

MQILFDSRSRNCKEPFGCIAAGEVLSLKLYIKDAGTPGVLFLLERDGGGTTEYPMHFCGE
KDGYRRYSCNLVMAEPGLYFYNFLVQGDGAAQAVYRDGHNKPCCGEGGKWQLTCYRAATL
PPEAFYGRVMYQIFPDRFNRAGQCGTSEKLTPFYVHENMTDTPVFRPDANGEILNNDFFG
GNFAGIRARLPYLAELGVTVLYLNPIFKAFSNHRYDTADYMEADPLLGTNKDFKELCDAA
HKLGMRVLLDGVFSHTGSDSVYFDIKNRFGGGAYHDPESPYRSWYQFEHYPDLYKSWWGI
KTLPCVEETDAGFLNYILEDDNSVIKYWLRQGADGWRLDVADELPDEFLSALYDTVKQEK
PDGLVLGEVWEDASNKISYGRRRRYLQGGILDSVMNYVWRDAIIRFVRGELSAEDLNESV
MSLCENYPPGSLHTMMNLLSTHDTPRILTLLGADNPPQSREERAGYTLSDEALAKAVDRL
SAAVFLLFTLPGSACIYYGDEIGMQGFEDPFNRAYMGDRAANGAISALFRKLAALKNRFD
ALKKGALTPSFCGDGLFGFYRAWGQECLFCAVNVSDVPHPIVTVGQEVIYENNTWQENGQ
RLLLPYGSIIIKGM

Enzyme Prediction     

No EC number prediction in MGYG000004064_00394.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	181	510	1.3e-123	0.9936708860759493

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	0.0	127	547	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	5.32e-118	121	576	115	560	maltodextrin glucosidase; Provisional
PRK14510	PRK14510	1.00e-88	14	546	14	576	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
COG0366	AmyA	5.82e-60	128	522	1	376	Glycosidase [Carbohydrate transport and metabolism].
cd11316	AmyAc_bac2_AmyA	1.87e-58	181	516	20	346	Alpha amylase catalytic domain found in 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 Chloroflexi, Dictyoglomi, and Fusobacteria. 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
CAB1239245.1	3.81e-169	4	612	1	613
QNK39367.1	8.97e-169	4	612	1	614
QAT48387.1	5.12e-167	4	612	1	614
QUO36689.1	3.45e-163	4	575	6	580
QCI59536.1	5.18e-162	4	586	6	589

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5BN7_A	9.16e-75	120	576	117	563	Crystalstructure of maltodextrin glucosidase from E.coli at 3.7 A resolution [Escherichia coli K-12]
2Z1K_A	1.73e-74	125	580	4	426	CrystalStructure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2Z1K_B Crystal Structure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2Z1K_C Crystal Structure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2Z1K_D Crystal Structure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8]
1J0H_A	4.13e-68	122	610	129	582	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	1.11e-67	122	610	129	582	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	2.15e-67	122	589	129	556	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
P38939	2.60e-92	6	561	256	845	Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P16950	1.21e-91	6	561	256	846	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P36905	2.01e-89	6	561	259	846	Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P38536	4.59e-84	6	561	259	845	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P21517	3.85e-74	120	576	115	561	Maltodextrin glucosidase OS=Escherichia coli (strain K12) OX=83333 GN=malZ PE=1 SV=5

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
1.000040	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004064_00394.