CAZyme Information: MGYG000001725_00584

Basic Information

• Species: Massilimaliae sp900752435
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Massilimaliae; Massilimaliae sp900752435
• CAZyme ID: MGYG000001725_00584
• CAZy Family: GH13
• CAZyme Description: Amylopullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
617	MGYG000001725_3|CGC2	71236.4	4.7627

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001725	2564044	MAG	Sweden	Europe

• Gene Location: Start: 80265; End: 82118 Strand: +

Full Sequence      

MKIYYDSKDLKYKQPFGCLRQDETCTLRIDIPKQNGAVEVAMVLETENGGFYQHYSLANR
VEEGDYVQFSGSFSLSECGLYYYYFQVNTNNSSFNVYKEGTRGTCITGQDKWQLTCFHKD
YDTPEDFKGKVMYQIFPDRFNRVGECDVHDKLQPFFIHENREDVPVYYPDHNGIVQNNDF
FGGNLQGIIEKLPYLQKLHVEILYLNPIFMAYSNHRYDTADYKRVDPLLGTEEDFKELCK
KAHACGMKVILDGVFSHTGCNSVYFDKYNVFGNGAYSHFDSPYRKWYQFHGETSQVYNSW
WGIDTLPCTEEMNEGYLDFIIRDEDSVLAHWLNLGADGYRLDVADELPDEFIELLNRRVK
EIKPDGLVIGEVWEDASNKISYSVRRKYFTNLELDSVMNYPYKDAIIGFVRGDQSAESLA
NTVMTIAENYPKPVLDCLMNILGTHDTMRILTVLGTDNFSLSRDEKAYASLNDGQMRVAM
DRLMAAAFLQFTLPGCPCIYYGDEAGSQGFEDPFNRRFFPWDHINEELLAFYQELTRVKA
AYEALQVGNIKVISHYPGVFIFTRTVGKKKMIAFVNLRDQYECFTTHPIVMLKNGTVSEE
QVVLGKYGFMLLEADAE

Enzyme Prediction     

No EC number prediction in MGYG000001725_00584.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	183	513	1.8e-121	0.9936708860759493

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	8.04e-177	129	550	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	8.29e-110	121	576	113	557	maltodextrin glucosidase; Provisional
PRK14510	PRK14510	2.72e-89	1	548	1	575	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
cd11316	AmyAc_bac2_AmyA	1.00e-60	170	548	15	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.
pfam00128	Alpha-amylase	6.88e-55	183	513	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
QCX33355.1	4.67e-165	4	566	6	573
CBK97234.1	2.12e-157	5	612	6	622
CBL33914.1	2.12e-157	5	576	6	577
QOX62807.1	2.54e-157	3	605	13	610
QGT51010.1	4.60e-156	1	566	1	572

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WC7_A	3.30e-68	123	576	5	432	Crystalstructure of Nostoc Punctiforme Debranching Enzyme(NPDE)(Acarbose soaked) [Nostoc punctiforme],2WCS_A Crystal Structure of Debranching enzyme from Nostoc punctiforme (NPDE) [Nostoc punctiforme],2WKG_A Chain A, Alpha Amylase, Catalytic Region [Nostoc punctiforme PCC 73102]
1J0H_A	4.41e-68	121	580	126	540	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	1.19e-67	121	580	126	540	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]
5BN7_A	2.11e-67	124	582	119	566	Crystalstructure of maltodextrin glucosidase from E.coli at 3.7 A resolution [Escherichia coli K-12]
2Z1K_A	4.95e-66	127	564	4	413	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P16950	1.50e-102	3	566	248	848	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P38939	2.15e-102	3	566	248	847	Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P38536	9.61e-95	3	610	251	884	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P36905	1.19e-94	3	610	251	885	Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P38940	2.41e-67	121	580	126	540	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT 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
1.000091	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001725_00584.