CAZyme Information: MGYG000004157_01090

Basic Information

• Species: HGM11514 sp900757255
• Lineage: Bacteria; Firmicutes_A; Clostridia; HGM11514; HGM11514; HGM11514; HGM11514 sp900757255
• CAZyme ID: MGYG000004157_01090
• CAZy Family: GH13
• CAZyme Description: Amylopullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
614	MGYG000004157_27|CGC1	71120.55	4.9221

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004157	2480742	MAG	United Kingdom	Europe

• Gene Location: Start: 12707; End: 14551 Strand: +

Full Sequence      

MNIIFDSRKKQYKSIFGSVPTEQEILFRISVGENISYAGLIANGCEFQMQPNNNGFFSVR
YTAPSQPQLVFYSFKIITNEQNILFYGNNEQQKGGVGKLYDASPVPYQLTVYDKNKSVPV
QYAGSVLYQIFPDRFYREGPVLSPKPNSMLHGGWDDLPFYIKDQDGKIKAWDFYGGNLKG
ITQKLPYLKELGIDIIYLNPIFEARSNHRYDTADYLKIDPMLGTEEDLAELAQSAKRLGM
KIILDGVFNHTGCDSIYFNKFGTYGTSGAYRDVDSPYYPWYTFEQYPDKYTCWWGVDDLP
MVDELDPSFLDYIIYDSGSVINKWMGLGVTGWRLDVADELPDEFIRRLKHKCIQNNPDTL
LLGEVWEDASNKISYDVRRTYFTRDELDAVTNYPFRNWMLEFLNDRITSQDLFENVMCQF
ENYPLHHFYLNANMLSSHDIERILTTVKNSTERTMQWLTILIGVQMTFPGMPLVYYGDEA
GVEGGVDPDNRRTYPWGHENQDIFQLYKTMIEVHRKHSVFHTGYLKPFFIADDIFGYFRY
FKNQKDVFGQTCGTDFAIVLINKNKSDCKRVSLKLPEYAPQSFTGLLDGEPCQNEEGCVF
IHLDPLQIKIIFGQ

Enzyme Prediction     

No EC number prediction in MGYG000004157_01090.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	176	489	2.9e-123	0.9968354430379747

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	0.0	124	525	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.
PRK14510	PRK14510	5.00e-110	12	564	12	621	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
PRK10785	PRK10785	5.88e-102	63	573	70	566	maltodextrin glucosidase; Provisional
cd11337	AmyAc_CMD_like	2.18e-60	178	523	27	326	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.
cd11353	AmyAc_euk_bac_CMD_like	4.76e-55	178	523	29	364	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANP70716.1	3.77e-189	6	579	8	577
AND86225.1	3.77e-189	6	579	8	577
QNB67648.1	3.77e-189	6	579	8	577
AKA69798.1	1.57e-185	1	614	4	643
AWI04092.1	2.23e-185	1	614	4	643

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Z1K_A	9.76e-73	122	523	4	397	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]
1BVZ_A	5.23e-70	125	613	131	583	Alpha-amylaseIi (tvaii) From Thermoactinomyces Vulgaris R-47 [Thermoactinomyces vulgaris],1BVZ_B Alpha-amylase Ii (tvaii) From Thermoactinomyces Vulgaris R-47 [Thermoactinomyces vulgaris],1JI2_A Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2 [Thermoactinomyces vulgaris],1JI2_B Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2 [Thermoactinomyces vulgaris],3A6O_A Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase 2/acarbose complex [Thermoactinomyces vulgaris],3A6O_B Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase 2/acarbose complex [Thermoactinomyces vulgaris]
1JF6_A	5.23e-70	125	613	131	583	ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF6_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]
1JF5_A	5.23e-70	125	613	131	583	ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF5_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]
1WZM_A	1.41e-69	125	613	131	583	ChainA, Alpha-amylase II [Thermoactinomyces vulgaris],1WZM_B Chain B, Alpha-amylase II [Thermoactinomyces vulgaris]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P16950	6.87e-112	67	614	329	921	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P38939	1.00e-111	2	614	247	920	Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P36905	3.82e-111	2	597	250	905	Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P38536	4.54e-109	2	584	250	889	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
Q08751	2.86e-69	125	613	131	583	Neopullulanase 2 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaII 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
1.000052	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004157_01090.