CAZyme Information: MGYG000002492_00977

Basic Information

• Species: Agathobacter rectalis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Agathobacter; Agathobacter rectalis
• CAZyme ID: MGYG000002492_00977
• CAZy Family: CBM82
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1368		151582.45	4.5126

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002492	3449685	Isolate	not provided	not provided

• Gene Location: Start: 985755; End: 989861 Strand: +

Full Sequence      

MRKLKERFHRKHGIFRQVFSLILVLAMIMTMIPSIGGNLVKAASTPMNVTIHFMKPSNWN
WTEPAVQFWGYNSIEVSNDANGGESKEIPGWGVSAYFFREGTETNTNGDKDYYLTVKSDT
TGFQFLDYKNTSNYKNPANDAKLTQYTEDTPTDVYYVAKDGSNFAYYLDPEGNTPVPDLP
ETETTFLLVGTLPGTGWDQNATPNFAKSETNENEYSISIKNVPAQTYEYKILEDPALNGW
GKAWTGESNVQLEVKAPADITMKLDKTDNDKKTDITISYIKTLDVKTPAQVEKGVDISLP
AKGTYYAGDTKGSKTEGVGVTYTAVSEGITVSGTTLKVPTSYKGTDVTIRAAYNGVKKDI
TIPVVDKVYTYTIYYHDFNASHMAADASSLWIWQDGGADGVLYNFSGTEQLSDENTWLKA
TVKLPYYKNIRIIPKNYGDTWSWKSEEISYDNTAKDENVTFYITSNSKEAYTTIPELVKP
RERYVMVEYDRPAGDYEGWNIFTWNSGFGEKVTVNFQKMNGKMVAKIPVKDTTADMMLSF
CMRRSTADDEWADKDGGDHYVSVPANQNVVKAKFVQGEGITEVLPSNIGCVLDGENGKIH
FYYRDDEMIAADNTQKSIADKVSVTINGVKHAMTYDAANERFSYDLTNITTGDYCYYYTV
DGVEKLDAYNAETKDYDGKTCSYRFYKKFDAAITAELSKSSMDYNDNNVLTIKTNPAEGA
DMSGFEVATATVDLSALGLSSTYAIDPELMEATISCLDTTTTGDKTLPVTVKDIYGNVYR
TSTNVTVTERDKKDGDFDWDEAVIYFAVTDRFFDGDKSNNDAYGVGDYDTSDKGGSSYHG
GDFAGLNEKLDYLKDLGVNTIWITPIVENITDDQPDAETGMHTYGYHGYWASDFTKLNKH
LGTEEEFAALIEAAHSRGMKLMVDVVLNHAGYGTENYFNNILKDEDGNTIKMLRDSSNTV
SGDDKQDALSDLPDFVTEDAEVRNQLIKWQTDWMEKYKIDYYRVDTVKHVDSTTWSAFKN
SLTIVNPDFKMIGEYSGAGYANTAGELGTGSMDALLDFDFNDFAKDFVGGKISTVENSLL
KRNAALNNTATMGNFLNNHDDDTLQELLVKKSGFSEEEAYNLMKVAATLQITAKGQPIIY
YGDELGQAGANDWPYQTNRRDFDWKELEAQKADSNSIYNHYKTMLSIRNAYTDVFARGSR
TSVLSSDEGGYDVIARSYGDTTLYVGMNINEKATEVTIPVSAEAGSKMENLYDGNEYTVS
ADKTVTVSIPAAKDGGTVILTEVKKTVDPTPADPGKKDPTPAPAKKDPTPAPAKKDGVIS
VTDKAAIETKKAAPKSGDDNEAATYVCLLGLAMVAITAATYRKKKACK

Enzyme Prediction     

No EC number prediction in MGYG000002492_00977.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	841	1150	1.6e-108	0.9931972789115646
CBM83	482	578	1.3e-44	0.9895833333333334
CBM82	49	177	2.6e-43	0.9838709677419355

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	3.20e-80	803	1191	4	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	1.99e-68	797	1220	185	672	alpha-amylase; Reviewed
cd11319	AmyAc_euk_AmyA	1.47e-66	798	1190	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.
cd11338	AmyAc_CMD	2.26e-57	801	1199	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.
cd00551	AmyAc_family	9.64e-55	803	1147	1	259	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
ACR74843.1	0.0	1	1368	1	1368
CAJ20070.1	0.0	1	1291	1	1412
CBK91127.1	9.96e-309	1	1367	1	1363
CBK93942.1	5.57e-308	1	1367	1	1363
QJX64947.1	4.10e-201	195	1294	54	1104

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	1.41e-52	799	1275	6	453	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	3.65e-52	799	1275	40	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	1.43e-44	799	1256	7	433	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
6SAU_A	3.62e-42	799	1262	24	442	ChainA, alpha amylase [Cordyceps farinosa],6SAU_B Chain B, alpha amylase [Cordyceps farinosa]
6SAO_A	8.80e-41	798	1275	5	430	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
Q05884	6.89e-42	828	1295	87	633	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
Q08806	1.25e-39	799	1269	38	485	Alpha-amylase 2 OS=Schwanniomyces occidentalis OX=27300 GN=SWA2 PE=3 SV=1
P25718	2.06e-39	781	1225	166	670	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
P38940	5.90e-38	798	1270	130	576	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
Q10427	1.20e-37	799	1195	19	387	Uncharacterized glycosyl hydrolase C11E10.09c OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPCC11E10.09c 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
0.083786	0.913210	0.001334	0.000841	0.000430	0.000407

TMHMM  Annotations     

start	end
13	35
1342	1361