CAZyme Information: MGYG000002159_00035

Basic Information

• Species: UMGS403 sp900540865
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS403; UMGS403 sp900540865
• CAZyme ID: MGYG000002159_00035
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1311		140108.23	4.5416

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002159	2536943	MAG	Germany	Europe

• Gene Location: Start: 31386; End: 35321 Strand: -

Full Sequence      

MKLRRSIVSVLLTAAMLMGCLIIPSLSASAAADTAGGTGAPVSEAASAAGNAAAYNLPSN
VQDGNIFQAFTWRFTDISKYMKEIAAQGFGSVQVSPVQPTAFKADGDNAASYMIDWWKYY
QPVDFKLGNGLGTKEDFKEMCEVAESYGVKVIVDIVANHMAQRDTGASYSKNLQIPEDLR
LDSSAWHVVNSNVNDNTRNDMTQKSLGGLPDLNTGSTKVQNYVKSLLKECLDSGADGFRF
DAAKHIELPSDSPSSNFWPNITSYIKSIKPDAYIYGEILKPCKTNDYSKYIKMTDSQLGA
NVRSAITSGNASSGVVNYSAEGASAKDIVAWVESHDNFCDGSSTKLTHQQLLLGWGIIGA
RKDSTSLWFCRPEHEQLESAGFIKYDEMIGGPGNTLWQDKTVAAVNQFRNNFAGQSEKVT
ASGSQFYVQRGTSGMVIVNLGGSNASINFTSTMANGTYKDQVSGGTFTVSGGRLTGSVPA
KSVAVIYNKTNTTPVTNVSLNGKKVTSDKTTYTGNSTGYYTNNYNFTSETATLSLSLQDA
KSGTYSVSGGKPVSFTGSTSVVIGKNVKSNTSVTVKVTATDGTRTTEETYVFVKKLSSDK
LTVYFDATGYETWAEYYCFVKTSGGSAVKAYPGFEMTKVSGNIYKAELTGVSGSAYVKFN
EGHVKTGLDGRTVPPTVVNFGSAATPANREKGGFLLNGSMIWQNGEWKDYGYSTDETPVD
PSNPTKPTETDPTKPTETDPTKPTNPDPGTKYMLGDVNGDGYVKLADVLEIQKHLASMLV
LNGTAYAAGDVNANGKLETADVLEIQKFLAGMGSRYDIGKYVGGGELPTIPTSTDPTEKP
TVTPGGSITLTLNKPASWGSDVYAYLFNGGGGKNAEWPGEAMTKSGNTYTITVPEDAAYD
KVIFSDSPYEAVDGTGAPKIAVRVQTAQLAVTEAPYTIEEVTVTAGSLSFTPTHVYLYNP
DPNSFAETNVWPGIAITGNSITVPAGVYTKAIFHDGTNQEEYDVEGSTPTDPTKPTDPVI
PGDDITLTLNKPASWGTDVYAYLYDGETKNAEWPGEPMTANGNTYSITVPSGLYSSVIFV
DSPETGTDPQGAPKVSARMQSASMDVQNGTYDIAMTTVSVPSDLGFTPTHVYCYNPGPEN
FAETGVWPGLALTGASIEIPAGVYTKAIFNDNGANEKPVDIEGSTPGPGPGPGPGPGPEG
TITIYFSNSVNWANVYLYAWRDSDENKNHEWPGVELVSVGKNSFGETIYSATIDTSEFDR
IIFNNGNGEQTQDIDLAGVTNNTGFYCDKSSQNSQGHYKYGMYEFDPSYIV

Enzyme Prediction     

No EC number prediction in MGYG000002159_00035.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	72	341	3.4e-83	0.9887218045112782
CBM26	1203	1273	3.7e-16	0.8933333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	1.06e-108	63	419	1	352	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 Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. 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.
cd11317	AmyAc_bac_euk_AmyA	3.45e-31	66	337	4	238	Alpha amylase catalytic domain found in bacterial and eukaryotic 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 AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. 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.
cd11320	AmyAc_AmyMalt_CGTase_like	3.42e-24	80	351	55	331	Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins. Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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.
cd11316	AmyAc_bac2_AmyA	2.32e-20	131	292	66	238	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.
cd11338	AmyAc_CMD	6.35e-19	131	278	99	239	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCT06294.1	4.90e-112	51	777	46	734
AWB44629.1	7.45e-98	55	605	50	573
QDY86356.1	5.17e-96	55	605	46	569
QUF82755.1	9.29e-96	62	1256	51	1179
AXB83939.1	1.25e-95	62	1256	51	1179

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UA7_A	2.44e-84	60	487	2	420	ChainA, Alpha-amylase [Bacillus subtilis]
1BAG_A	6.88e-84	60	487	5	423	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
3DC0_A	8.63e-84	60	487	2	420	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1VIW_A	3.00e-22	65	349	12	300	TENEBRIOMOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX [Tenebrio molitor]
1CLV_A	5.33e-22	65	349	12	300	YELLOWMEAL WORM ALPHA-AMYLASE IN COMPLEX WITH THE AMARANTH ALPHA-AMYLASE INHIBITOR [Tenebrio molitor],1JAE_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE [Tenebrio molitor],1TMQ_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR [Tenebrio molitor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	2.09e-84	41	698	28	646	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	5.58e-72	57	489	47	463	Alpha-amylase OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=amyA PE=3 SV=2
P30269	1.32e-58	60	489	144	608	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P29750	1.17e-25	54	487	31	481	Alpha-amylase OS=Thermomonospora curvata OX=2020 GN=tam PE=1 SV=1
P56634	2.92e-21	65	349	12	300	Alpha-amylase OS=Tenebrio molitor OX=7067 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000823	0.591777	0.405780	0.001011	0.000373	0.000211

TMHMM  Annotations     

start	end
7	29