CAZyme Information: MGYG000002230_00078

Basic Information

• Species: Ruminococcus sp900545125
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus; Ruminococcus sp900545125
• CAZyme ID: MGYG000002230_00078
• CAZy Family: GH13
• CAZyme Description: Amylopullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
628	MGYG000002230_3|CGC1	72998.8	4.8251

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002230	2337720	MAG	United States	North America

• Gene Location: Start: 13780; End: 15666 Strand: +

Full Sequence      

MKPIYDSWDLSYKSIFGAIKQGETCRFTIRLAKDIPLESPPVLVLFRTGFKERFLRMNEV
TDEGDCMAYSTEYTARYTDVHYYYFSYISNGARHYIKKQNVHEGNVDFGDLFQLTVYNNT
YETPDFLKGGVMYQIFPDRFCKSGKEHEGVPGDRVMREWGETPYYKPDQNGHVWNNDYFG
GDFAGIQSKLPYLHDLGVTCIYLNPIFESHENHRYNTANYMKADPLLGTNDDFEELCREA
DKYGISVILDGVFSHTGADSVYFNKFGRYPEQGAYQSKDSPYYSWYTFINYPDVYEAWWG
IDTLPNVWENNEDYTEFICGEEGVLNYWLGKGAAGWRLDVADELPDRFLFNLRKSVKGYG
KDKIVIGEVWEDASNKESYGIKRRYLLGNQLDSVMNYPFREAIINFVKGGKANDLANSVM
TIAENYPKPTLDVLMNFVSTHDIERAINRLGGESCDDKSKDWMAERYLNEYEYNLGKNRL
KAAMALMFFLPGVPSIYYGDEAGLQGYKDPFNRRCYPWGNEDHELIEYVSRLSRVRKSIP
NLRDGRIYFVDNDKWVNDDRVTVFTRQGDPDYIFFVNKSEADITVGNVSKLLELFSDLKP
YIGRFENNTVEIEPYGYTIITGNFLRLF

Enzyme Prediction     

No EC number prediction in MGYG000002230_00078.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	181	510	1.1e-129	0.9936708860759493

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	0.0	129	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	2.03e-92	21	567	17	546	maltodextrin glucosidase; Provisional
PRK14510	PRK14510	2.92e-84	73	545	49	575	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
cd11316	AmyAc_bac2_AmyA	9.49e-60	181	545	20	403	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.
cd11337	AmyAc_CMD_like	8.84e-49	190	546	34	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
CBL33914.1	4.25e-251	3	620	4	622
CBK97234.1	3.45e-250	3	620	4	622
BCI61467.1	4.65e-196	5	615	6	610
CAB1243760.1	5.49e-196	4	545	1	547
QQR32000.1	5.04e-193	4	620	1	622

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Z1K_A	2.02e-70	128	551	5	406	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]
5Z0U_A	6.29e-69	121	545	124	543	Thermoactinomycesvulgaris R-47 alpha-amylase I (TVA I) 11 residues (from A363 to N373) deletion mutant (Del11) [Thermoactinomyces vulgaris]
5Z0T_A	2.10e-67	121	545	124	554	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]
1JI1_A	4.01e-66	121	545	124	554	CrystalStructure Analysis of Thermoactinomyces vulgaris R-47 alpha-Amylase 1 [Thermoactinomyces vulgaris],1JI1_B Crystal Structure Analysis of Thermoactinomyces vulgaris R-47 alpha-Amylase 1 [Thermoactinomyces vulgaris],1UH3_A Thermoactinomyces vulgaris R-47 alpha-amylase/acarbose complex [Thermoactinomyces vulgaris]
1IZJ_A	5.56e-66	121	545	124	554	ChainA, amylase [Thermoactinomyces vulgaris]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P36905	2.31e-101	5	561	258	848	Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P38939	5.86e-99	5	545	255	829	Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P38536	8.52e-98	5	582	258	873	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P16950	4.66e-97	5	545	255	830	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
Q60053	3.76e-65	121	545	153	583	Neopullulanase 1 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaI 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
1.000072	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002230_00078.