CAZyme Information: MGYG000000489_00796

Basic Information

• Species: Agathobacter sp900548765
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Agathobacter; Agathobacter sp900548765
• CAZyme ID: MGYG000000489_00796
• CAZy Family: CBM82
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1543	MGYG000000489_4|CGC3	169086.02	4.3565

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000489	2786257	MAG	Fiji	Oceania

• Gene Location: Start: 170990; End: 175621 Strand: -

Full Sequence      

MRKVKEHFHKKQGIFRRVFSLILVLAMIMTMIPSIGGMATAYADGTSPTIRLYLDKPSTW
NTPVVNVWAPGATVDNHGAGNATISQWGDQEKPKLAHEESSGLYYVDVQSSEWTGFQFVD
AGSAEKAAPDIKTEGAAIEQIKTFTSDTSIYCLLDDNGKYQWYKDASKNETLIPESVPTE
CDLTINYKSTLGNDVAAYIYHETNKPAGEWPGKTMTAAEGHEGWYTMHLTLDNSTDYELI
LNDDGHGNQLETVTLSTKGKAEAEYWFDGSLSETKPADWKYVTTIHYLASGMGSTIYNHM
WGADASATGAGVGKDWPGGQISENADHSGWYDVVYTQDVKQNFSCIFNNNSGAQTDNIDV
SVTSTSTELWVTGTKSGGDTTVYKTAPDSWEAPVPDHTFTMYYYNEDLSTDTDMGKVDMW
MWNAGLNGSYVFDETEYDAANNVTWFKKTITVAGSNVGKTVGLKARYDITQGWDGGSDTA
DRSFTISGEENEVLYYVDGSNPVHKKPVIVPTEKRYLVLDYENPGLKEKGITPQFYTWSS
GYASALTDFTYVGGDKWTITIPAKPSCTKVDFCIALDSTVDPWIKDGGDHSVTFPSDQKV
IYASMKAGSEPEIAMPYNTGYEVDAEKQQVSYYYRDDAAFVDGTLKDMTVAVDVNGTEYP
MTYNDTTKRFEYVKSGLTDGKTHYRYKANGTYVVDAFNSNSEKYNEADYSYFEYYKLNAT
VTAEVMNESFNYNENNVVKFNVKQADTDTQKLEVASASIDVSSLGGSSEMPIEPELQAVT
ISATVDTTLGTKTLPITVTDQYGNKFTTTVDVKIVDRVKENKNDFDWDESVVYFMVTDRF
FDGNESNNTASGADTYGDNEGLYHGGDFAGVTAKLDYLQDLGVNTIWITPIVENVKGVAV
TDKGSEDVPYNAAYHGYWASDFTKLNPTLGTTEEFETMISEAHNRGMRIMVDIVVNHAGY
GTESTFADMLRNKSVSEGDIKSWQSGLPDFATENADVRAKLVEWQTSWMKDYGVDYFRVD
TVKHVDSTTWAALKNSTTEVNPSFKMIGEYFGAGYASNGSTLGTGQMDADLDFDFNDQAT
SFVSGNISSVEKFLSARNSALNNTYMTGQFLSSHDEDGFKAALMNGKGYTEDEATAAALV
AATLQLTAKGIPVIYYGEEVGLSGLNNYPYQTNRYDMDFSLATEDNVTYQHYKTMLSIRN
AYTDVFARGSRTSILSSDEDGYDVIARSYGDTTLYVGMNINEKATEVTIPVSAEAGSKME
NLYDGKEYTVSADKTVTVSIPAAKDGGTVVLNAVKTAIIPDDNNNGNSGINLNITVDGSD
FTEVVNTINAVSDGTTVIVNVNGTTAIPEDVFNSMSGKDVNVVFKVGENATWVVKGKDIK
NKLSKAIDLGVTLGKSGIPSDKIKALAGDNAFIELSLAHDGEFGFTATLRLYVGTQYNGK
YANLYYYNEKTGSLEYVKAVKVNADGAVEYEFVHASDYVIVMSNADMKPADAAPATPTAN
PTPADQKGSSVATGDKTPIVQTAAILIIGGCVLFVAYRRRKRV

Enzyme Prediction     

No EC number prediction in MGYG000000489_00796.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	866	1165	1.2e-109	0.9931972789115646
CBM82	50	173	1e-47	0.9838709677419355
CBM83	514	609	4.4e-45	0.9895833333333334

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	8.07e-73	829	1202	2	344	Alpha amylase catalytic domain found in 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 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.
PRK09505	malS	4.61e-70	825	1231	185	672	alpha-amylase; Reviewed
cd11319	AmyAc_euk_AmyA	1.50e-61	826	1201	5	371	Alpha amylase catalytic domain found in 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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	9.87e-61	831	1199	6	387	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.
cd00551	AmyAc_family	1.76e-52	831	1156	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
CBK91127.1	0.0	1	1295	1	1291
CBK93942.1	0.0	1	1295	1	1291
CAJ20070.1	0.0	1	1541	1	1672
ACR74843.1	3.03e-289	1	1300	1	1289
QKH63022.1	8.61e-169	397	1291	213	1103

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6B15_A	7.36e-132	182	391	2	209	ChainA, Amy13K [[Eubacterium] rectale DSM 17629],6B15_B Chain B, Amy13K [[Eubacterium] rectale DSM 17629],6B15_C Chain C, Amy13K [[Eubacterium] rectale DSM 17629],6B15_D Chain D, Amy13K [[Eubacterium] rectale DSM 17629],6B3P_A Chain A, Amy13K [[Eubacterium] rectale M104/1],6B3P_B Chain B, Amy13K [[Eubacterium] rectale M104/1]
6AZ5_A	1.46e-67	395	510	1	116	ChainA, alpha-amylase [[Eubacterium] rectale DSM 17629]
5A2A_A	3.03e-52	822	1286	1	453	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	5.84e-52	821	1286	34	487	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis],5A2C_A Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
4E2O_A	2.47e-46	822	1247	2	407	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	3.33e-39	825	1236	184	670	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q08806	1.59e-38	827	1280	38	485	Alpha-amylase 2 OS=Schwanniomyces occidentalis OX=27300 GN=SWA2 PE=3 SV=1
P21567	4.53e-37	819	1280	25	475	Alpha-amylase OS=Saccharomycopsis fibuligera OX=4944 GN=ALP1 PE=3 SV=1
P31747	1.12e-36	821	1241	42	471	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 6.6.3) OX=29335 GN=cgt PE=3 SV=1
P30920	3.50e-36	816	1241	37	471	Cyclomaltodextrin glucanotransferase OS=Niallia circulans OX=1397 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
0.001561	0.997278	0.000287	0.000431	0.000228	0.000197

TMHMM  Annotations     

start	end
21	43
1518	1537