CAZyme Information: MGYG000003694_01410

Basic Information

• Species: Agathobacter faecis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Agathobacter; Agathobacter faecis
• CAZyme ID: MGYG000003694_01410
• CAZy Family: CBM83
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1507		165660.61	4.8428

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003694	3443393	Isolate	China	Asia

• Gene Location: Start: 157746; End: 162269 Strand: -

Full Sequence      

MGERRFSTKNRFVSFLLAIAMVLTLLPIGAVQAKAEDATVKLYFELPDGTTVTDWGVNVW
SAAKVSKGDTENAFRPKTWGTTGDKYPTLLADQTNKGWGYVEISGTIDGLQFVNTDGKEY
KCWNAQIANEGHKEAYFDPSVEKWYTSTEKTTEIKAAEIKNTFTLAGDSELTGNSKWDAN
DTRNVLMQDDSNENKFSITFHNVAKGTYSYKILQDPKNCGWDKPWGYGTGSDGNRSVTVE
APSDVTFTIDLTDASKNVEVIQKKLKKLVVDNGNISKGKAKELKISAKYYDGTSADANDV
NVSYRLKEEIAGVTLKDNTLSVAKDTSLTEVTVIVSYGDFEQELTIPVVEKQYQVTINMY
SQDLEMKPEVSDIYIFENGGDNNTTVTLDKTVEDAENNVTWVQGTVTVPYNSLGIIARDQ
AGSWDGGKDGNQYYVIDENTSEVTLWYVYGKTPVTKKPTITKEDPRYFYLEYENDTLTTI
PEFYSWTTGFAAELKKFESAGAGKWKIKVPVKSSCTKVDFVIAVDSSGSDWVKDGGDHSI
AFPEDQNVVCANMKQGEEPVLSAPYNKGYEVLPKENKIAFYYRDDNALIDDKLADMKVSV
DINGTEYEMTYNAGNKRFEYNYNKLESGRTYYRYKVGDEYILDKYNDKQEQKEGNDYSYI
EYYKLNATIQAEVMNASFNYNENNVVKFTVNQDENDTKKMEVASASIDVSSLGGSSTLAI
VPDLQAVTISATTDTSLGKKTLPIVVTDQYGNEYSTSVQVEVTARTKKNAKDFDWDESVI
YFMVTDRFFDGNESNNTASGAQTYGKDNAGLYHGGDFAGITQKLDYLEDLGINTIWITPI
VENIPGVTVTDTGKEDVPYNAAYHGYWASDFKKLNPTLGTEEEFQTLIDQAHNRGIRIMV
DIVVNHAGYDTDFGDMIRSGDDIVSGSDQKDSLSNLPDFRTEDPAVSAQLVKWQTQWVKD
FGIDYFRVDTVKHVENDTWAELKNALTEVDSDFKMIGEYAGGGYASNGNTLGTGEMDSDL
DFDFNDQATNFVKGNISSVESFLTSRNSVLNNTYMTGQFLGSHDEDGFKKKLLDGGMAED
AATAASMVAASLQITAKGQPVIYYGEEIGLTGLNNYPYQTNRYDFDWTMVNSDNKTYQHY
KKMLSIRNAYTDVFARGDRKTILASDENGYDIVSRSYKGTKLYVGLNIKDVAQTVEIPVS
ENNGTVLKDLYSGKTYTVSNGKIKVIIPAATDGGTVVLKNNSSTNGGSTGGSSSSGSTTT
ETKPSEDTKKDATTTESVIPAEKLPEGTTATVTVTKDASGKVTAEAAVAATGKTSKTGVK
ATVNADVIQAVTEAAGTKDVTITQEVKKADGTTAYTLQVNAADVKAGAKLAVMKKDEKTG
ELVLVNQKAYKVAKDGSVSLTFKGEGTYVVKTQAEVKAEAKQIAKTVKPAKTTVNVAAKK
TTVFKWNKKLNMENVAKITYKSSKKSVVSVNKNGKITGKKKGTGKVTAEVTLKDGTKKTV
KMKVKVK

Enzyme Prediction     

No EC number prediction in MGYG000003694_01410.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	815	1113	1.4e-103	0.9931972789115646
CBM83	466	557	5.5e-24	0.9791666666666666

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	1.19e-77	777	1150	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	1.39e-76	704	1184	91	677	alpha-amylase; Reviewed
cd11319	AmyAc_euk_AmyA	1.66e-66	774	1149	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	9.73e-66	779	1147	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.
cd11338	AmyAc_CMD	2.61e-56	777	1158	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
CBK91127.1	0.0	3	1233	9	1282
CBK93942.1	0.0	3	1233	5	1282
ACR74843.1	1.53e-266	3	1233	9	1275
CAJ20070.1	1.04e-243	3	1233	9	1397
QKH63022.1	3.62e-177	185	1233	73	1098

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	1.46e-45	775	1231	6	442	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	3.48e-45	775	1231	40	476	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	2.45e-43	775	1213	7	431	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
1J0H_A	1.29e-37	774	1228	130	576	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	3.09e-37	774	1228	130	576	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	9.46e-44	773	1170	184	659	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
P38940	7.04e-37	774	1228	130	576	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
P21567	4.71e-36	767	1166	25	418	Alpha-amylase OS=Saccharomycopsis fibuligera OX=4944 GN=ALP1 PE=3 SV=1
P31747	5.95e-36	769	1112	42	402	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 6.6.3) OX=29335 GN=cgt PE=3 SV=1
P21543	8.60e-36	774	1227	743	1186	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 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
0.000279	0.999066	0.000164	0.000175	0.000145	0.000132

TMHMM  Annotations     

start	end
12	31