CAZyme Information: MGYG000000136_01879

Basic Information

• Species: Agathobacter sp000434275
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Agathobacter; Agathobacter sp000434275
• CAZyme ID: MGYG000000136_01879
• CAZy Family: CBM82
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1431	MGYG000000136_10|CGC1	158179.83	4.6458

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000136	3864408	Isolate	Canada	North America

• Gene Location: Start: 34049; End: 38344 Strand: +

Full Sequence      

MRGERLKKRNRIISFVMAIAMVLTLVTVAPVTAQAAGVTNITIHFKNDWGWGTPALQYWD
GTSTTVIGGATEEVPGWGGAKATMLNKDAENEGWYTITLQGNCDGFQLLDFSKPSDNTNG
NVRTLAMDYCNDKEPTDIYFNCEKFLTKEDPWYLDSNFQTSIETKLPKQEEETYDPATLV
GDFSALTFTNEDEKIGNWNPADTNGDMVYVGNDVYAKTIHFKPLNEEASVQYKVAFNHAW
DESIGENGTSDNVTLSIPAGTSYLTVVCDHKNRNLYNSVTNGADTTGDTVSIIGTVRDNN
TWVETYEGTEYDFVKLSNRYYVYQKAFKAGSYQYKAVFNHKDWASWDNITLKLLNDKVVT
FVYDAETGNAYDSVNNLDKVIEALTAEPQNIEKRWALVEYDRLDGDYEGWNIYCWNSGFS
DGLNVKVDEFNGKHYLRIPVKASEADMTLSFCMRKSTTENEWAEKDGGDHYITFPADQKV
VIAKFQQGQGITSVLPYNKGYEMKGAENKVAFYYRDDALMQELNESSLSDKVSVVVNGTT
YPMTFDKDNQRYVYELEGCTSGKYMYRYIVNGEEVVDPFNESGAFSYKHFDDLTLEASFG
NATMDYNDNNVLSVSFKGTDATNIDAKSELASITADLSELGGKTLDVNTELLELSASVRD
SVSAGNKSVPVVAKDIYGNVYRATAEVTVTKRDTDTFDWDEAVIYMTCTDRFFDGNTKND
EGVNKSGSLSYHGGDFAGLEQKLDYLQNLGVNTIWITPIVENVDTDTDNGYHGYWAKDFT
KLNPYLGTEEELESLINALHKRGMKLMVDVVLNHAGYGTEDYFNSILKDQDGNSISMIRD
KDTTITGDDVRDSLSGLPDFVTENADVRNQLVEWQTEWMTKYDIDYYRVDTVKHVDATTW
AAFKNSLTKANPDFKMIGEYAGAGYANTAGELGTGTMDSLLDFDFNDKAEAFVTGDINSV
ESFFQSRNASIDNTATMGGFLSSHDEDSLVDKLITEKNLTEEEALKVFKVAAALQLTAKG
QAVIYYGEEIGQHGLNNYPIQSNRYDFDWNQVDTQSADANSMLNHYEKLLSIRTEYKKLF
ARGDRSSVLASDDDGYDVFTRSYNGTKLYVGLNIKDADQTISIPVSEAAGSTMTDLYSGK
IYTVSTDGKVEITIPKAVDGGTVILKKETSSNGGSSSSTGTTETVKNDTTTVTNPDGSKT
ETTVIKDLPADTKASLNVTTDANGNKTSEAAVETKGTEKKSGVSTSVSADVVKAITDKAK
TTDVTIKQEVKKADGSTAYTVEVSAGDVKAGETLKLLKKDAKTGELVLVNKKDYTVSADG
SVDLTIKNSGEYVLLNSKDAKAAVKEIKKTVKATKTSTNVKKKKTTKFPWSKKLNMENVD
KITYTSSKKSVVTVNKNGKITAKKKGTAKVKAVVTLKDGTKKTVTMKVKVK

Enzyme Prediction     

No EC number prediction in MGYG000000136_01879.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	734	1034	2.1e-105	0.9897959183673469
CBM83	393	489	2.1e-32	0.9895833333333334
CBM82	41	160	1.7e-18	0.9596774193548387

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	1.05e-74	703	1065	4	328	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	5.22e-72	697	1110	185	677	alpha-amylase; Reviewed
cd11319	AmyAc_euk_AmyA	1.09e-62	698	1047	5	361	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	5.52e-55	703	1029	6	348	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.
cd11338	AmyAc_CMD	3.31e-54	701	1084	1	388	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
CAJ20070.1	0.0	34	1165	175	1402
ACR74843.1	0.0	10	1165	16	1280
CBK93942.1	1.72e-227	4	1165	6	1287
CBK91127.1	1.31e-226	360	1165	479	1287
QKH63022.1	2.74e-176	400	1165	333	1103

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	8.65e-50	699	1156	6	440	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	2.18e-49	699	1156	40	474	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	1.22e-46	699	1123	7	409	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
6SAU_A	2.56e-40	695	1154	20	449	ChainA, alpha amylase [Cordyceps farinosa],6SAU_B Chain B, alpha amylase [Cordyceps farinosa]
6SAO_A	4.20e-40	698	1145	5	419	Structuraland functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Thamnidium elegans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	1.65e-40	691	1110	175	670	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q08806	7.93e-39	683	1129	19	489	Alpha-amylase 2 OS=Schwanniomyces occidentalis OX=27300 GN=SWA2 PE=3 SV=1
Q05884	7.38e-38	731	1155	95	603	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
Q10427	2.32e-37	699	1101	19	409	Uncharacterized glycosyl hydrolase C11E10.09c OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPCC11E10.09c PE=3 SV=1
P21567	2.94e-33	687	1037	21	367	Alpha-amylase OS=Saccharomycopsis fibuligera OX=4944 GN=ALP1 PE=3 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
0.000317	0.998901	0.000178	0.000228	0.000179	0.000161

TMHMM  Annotations     

start	end
12	34