CAZyme Information: MGYG000002290_01938

Basic Information

• Species: Sellimonas sp002161525
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Sellimonas; Sellimonas sp002161525
• CAZyme ID: MGYG000002290_01938
• CAZy Family: CBM34
• CAZyme Description: Neopullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
586	MGYG000002290_11|CGC2	69607.8	4.8851

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002290	3837069	Isolate	China	Asia

• Gene Location: Start: 101134; End: 102894 Strand: +

Full Sequence      

MDFTGVYHRTTEQMSYSLNESELIVNLKTGYDVKRVFLYYGDPFEAGILGGNEKWTGVRE
EIVYKKRLKHQIWWTTTLVPKYKRCKYYFELHTDDEVWYYFEDGFLTKEQMEMDGRMLQC
FTVPWMNPADVNRTPDWVNDTIWYQIFPDRFCNGTPGDDREGILPWKNEGEVKNEERYGG
NLEGIRQKLPYLKELGITGIYLNPIMEADSNHKYDTKDYTKIDPQFGDSETMKRLVAEAH
EHGIRVMVDAVFNHCGKDFAPWLDVKKNGRDSAYADWFMVNDWTMLNKEASTRDGRYYSF
AFADKMPKLNTNSESVISYFQDICEGWIRDYDIDGIRFDVGNEVSHRFLKRIRDHVKAIK
PDIYLLGEIWHDASQWLMGDEYDSVMNYPLMSGIHDFFIDPTMKKEDFEYMINHCYTMYM
QQSNNVLFNLLDSHDTERLMNRFHDLDLFYQQLAILFTMPGSPCIYYGTEIAMEGSFDPD
CRRCMPWDLIQTEENQQKIHEIQKLIHLRKTEPALRSLYFHFPEEYDEPRLVQYIKLDQE
QNKIEILLNCTEEPVTVKGEGEILFQRQYQDGRLEPKGVLIRRIGR

Enzyme Prediction     

No EC number prediction in MGYG000002290_01938.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	180	479	2.4e-115	0.9966666666666667
CBM34	6	131	1.4e-18	0.9916666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	0.0	140	520	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	8.80e-106	87	517	78	528	maltodextrin glucosidase; Provisional
cd11353	AmyAc_euk_bac_CMD_like	5.60e-89	140	516	1	362	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.
cd11337	AmyAc_CMD_like	1.83e-79	142	516	1	324	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.
pfam00128	Alpha-amylase	1.42e-75	180	479	1	334	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHB23531.1	0.0	1	583	1	582
QRT29813.1	0.0	1	583	1	582
QEI31023.1	0.0	1	583	1	582
QUI96246.1	0.0	1	584	1	584
AYA99649.1	0.0	1	584	1	584

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1J0H_A	4.04e-143	5	547	5	535	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	1.14e-142	5	547	5	535	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	1.28e-141	5	564	5	555	CrystalStructure Of A Maltogenic Amylase [Thermus sp. IM6501],1SMA_B Crystal Structure Of A Maltogenic Amylase [Thermus sp. IM6501]
1GVI_A	2.04e-140	5	564	5	555	Thermusmaltogenic amylase in complex with beta-CD [Thermus sp.],1GVI_B Thermus maltogenic amylase in complex with beta-CD [Thermus sp.]
1EA9_C	3.48e-134	1	549	1	533	Cyclomaltodextrinase[Bacillus sp. (in: Bacteria)],1EA9_D Cyclomaltodextrinase [Bacillus sp. (in: Bacteria)]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P38940	1.25e-141	5	547	5	535	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
P32818	3.30e-141	5	555	5	544	Maltogenic alpha-amylase OS=Bacillus acidopullulyticus OX=28030 PE=3 SV=1
A0A7U9P668	1.40e-140	5	564	5	555	Cyclomaltodextrinase OS=Geobacillus thermopakistaniensis (strain MAS1) OX=1408282 GN=T260_08735 PE=1 SV=1
Q59226	1.25e-133	1	549	1	533	Cyclomaltodextrinase OS=Bacillus sp. OX=1409 GN=CDI5 PE=1 SV=1
Q08341	2.43e-133	5	557	6	543	Cyclomaltodextrinase OS=Lysinibacillus sphaericus OX=1421 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 MGYG000002290_01938.