CAZyme Information: MGYG000001757_02073

Basic Information

• Species: Ruminococcus sp900540005
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus; Ruminococcus sp900540005
• CAZyme ID: MGYG000001757_02073
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
628		72678.54	4.7665

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001757	2373085	MAG	Sweden	Europe

• Gene Location: Start: 4324; End: 6210 Strand: +

Full Sequence      

MKPIYDTWNLSYKSIFGAIEQFQDCQFTIRLPKDIRPDFPPVLILFRTGFKERFLNMNKI
TEEDDCFAYTTEYNARYSDVHYYYFSYTQGGIRHYIKKVNVHEAAIDHGDLFQLTVYSNT
YETPDFLKGGVMYQIFPDRFCKSGKVHENIPEGRVLRDDWGGTPYYKPDQNGHVWNNDYF
GGDFAGIQSKLPYLHDLGVTCIYLNPIFESHENHRYNTANYMKADPLLGTNDEFAELCAE
AKKLGISVILDGVFSHTGADSVYFNKFGRYPELGAYQSKDSKYYEWYSFIDYPEVYEAWW
GIDTLPNVWENNESYTEFICGEDGVLNYWLSKGAAGYRLDVADELPDEFLNNLRKCVKNY
DKEKIIIGEVWEDASNKESYGVKRRYLLGDQLDSVMNYPFREAIINFVKGGSCHDFINSV
MTILENYPQPTVDVLMNFVSTHDIERAINRLGGENCDDKSKDWMAERYLTPEQYAHGKNL
LKAAMALQFFLPGVPSIYYGDEAGLQGYKDPFNRRCYPWGHEDKELIAYVSELSRVRKSI
PNMKNGRAYFVFNDTDTIDDRLIGLARQGEDIDYICFVNRSDASVSIPVLSSYLPRFTDF
APYYGEYADDTLTVAPYGYTIIKAKFLG

Enzyme Prediction     

No EC number prediction in MGYG000001757_02073.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	182	511	1.9e-129	0.9936708860759493

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	0.0	129	546	1	387	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	3.61e-87	117	589	109	568	maltodextrin glucosidase; Provisional
PRK14510	PRK14510	1.70e-82	112	538	97	567	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
cd11316	AmyAc_bac2_AmyA	7.49e-56	182	515	20	343	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.
cd00551	AmyAc_family	1.64e-45	131	499	1	253	Alpha amylase catalytic domain family. 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; and 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 this 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	6.02e-251	3	622	4	622
CBK97234.1	1.40e-249	3	622	4	622
BCI61467.1	3.87e-200	112	617	114	610
CAB1243760.1	2.02e-193	4	546	1	547
QNK39367.1	2.42e-191	103	623	101	614

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Z1K_A	8.86e-65	128	544	5	395	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	1.08e-63	121	589	126	546	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]
1JF6_A	1.96e-63	118	546	119	503	ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF6_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]
1J0J_A	2.89e-63	121	589	126	546	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]
1BVZ_A	5.24e-63	118	546	119	503	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P36905	1.32e-96	112	589	371	879	Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P38939	7.33e-95	112	591	368	868	Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P38536	3.76e-93	112	589	371	878	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P16950	1.15e-90	112	583	368	873	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P32818	4.11e-64	118	589	123	548	Maltogenic alpha-amylase OS=Bacillus acidopullulyticus OX=28030 PE=3 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
1.000057	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001757_02073.