CAZyme Information: MGYG000000681_00005

Basic Information

• Species: Lactococcus_A raffinolactis
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Lactococcus_A; Lactococcus_A raffinolactis
• CAZyme ID: MGYG000000681_00005
• CAZy Family: GH13
• CAZyme Description: Amylopullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
593	MGYG000000681_1|CGC1	68519.17	4.7745

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000681	1472277	MAG	Kazakhstan	Asia

• Gene Location: Start: 2558; End: 4339 Strand: +

Full Sequence      

MAEITYNSWLQEHKRPFGAVLVGTTVEFDLMIQTQNQVAVNIVLQFENGFKSYEKMTAIS
DGVFRMTLPNLTEIGFYNYYFQITEFDDTHEYRYFYGATDIGGGPGTTYVDEISVIPYTQ
TIFLKREKAPDWYRQAIFYQIFPDSFAKKGHLENPKDNIFFYGKETDSPYYIREANGDIT
HWTYYGGNLAGIIDKIPYLKSLGITALYLNPIFEARSSHRYDTSDYMKIDPVLGTESDFK
LLVDTLHQEGMHLILDGVFSHVGRNSKYFDFDGKSGGQGAYQTTQSPYFDWFTFNQYPDD
YKSWWGIKDLPTIDKTKESFQQYIYGECDSVLSKWNDLGIDGWRLDVADELPDVFIKGIR
DTLENYPEQVLIGEVWEDASRKVAYNQHRKYIYGDALHATMNYPFRDIILGLVRGEMTPE
TVARKLMQLSENYPTDVFLNNFNNIGTHDTERILTQLGQNLTKLDLAVGLLMTLPGVPTI
YYGDEAGLVGHKDPENRAFFPWENVNESTRKIYQKWIKIRQSASVLTTGNLSLFYSDRIF
GLIRDDSHETAVFVFNISNQGMMVDLNDMTFLNKKVDYPAFFLGAFESVYKFK

Enzyme Prediction     

No EC number prediction in MGYG000000681_00005.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	187	494	1.2e-123	0.9936708860759493

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	0.0	135	531	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	3.14e-103	130	564	116	565	maltodextrin glucosidase; Provisional
PRK14510	PRK14510	2.51e-73	16	533	15	579	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
cd11316	AmyAc_bac2_AmyA	1.28e-63	136	529	1	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	3.90e-58	187	494	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
CEN27753.1	0.0	1	593	1	592
QDJ28567.1	0.0	1	593	1	592
QIW61718.1	1.04e-300	192	593	1	402
QIW57202.1	9.88e-299	192	593	1	402
ATC62386.1	9.88e-299	192	593	1	402

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5BN7_A	4.10e-74	130	567	119	560	Crystalstructure of maltodextrin glucosidase from E.coli at 3.7 A resolution [Escherichia coli K-12]
1J0H_A	1.69e-72	128	560	127	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]
1JF6_A	2.20e-72	130	561	125	536	ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF6_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]
1BVZ_A	3.07e-72	130	561	125	536	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]
1JF5_A	4.29e-72	130	561	125	536	ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF5_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P36905	2.62e-81	14	584	266	897	Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P16950	7.25e-81	14	537	263	838	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P38536	1.99e-79	14	578	266	890	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P38939	7.29e-79	14	537	263	837	Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P21517	1.73e-73	130	567	117	558	Maltodextrin glucosidase OS=Escherichia coli (strain K12) OX=83333 GN=malZ PE=1 SV=5

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
1.000056	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000681_00005.