CAZyme Information: MGYG000002596_00243

Basic Information

• Species: Mediterraneibacter sp900555215
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter sp900555215
• CAZyme ID: MGYG000002596_00243
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1537	MGYG000002596_4|CGC1	166425.56	4.087

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002596	2662706	MAG	China	Asia

• Gene Location: Start: 6665; End: 11278 Strand: -

Full Sequence      

MVLKMWTIYKGEREKRMDYSKNSKKKNGLKARLVALLLATGLVLTGLPAGQAQAAPETAV
QTMAASSNISAASQYGLTEEIKDGAILHCWCWSFITIKNNMRDIAEAGFSTIQTSPANTC
NDTHPNMKIMGNDTVNGTDGCWWWHYQPTDWKIGNYQLGTRDDFKAMCDEADKYGIKVIV
DVIPNHVTPDLDEVSQDLYNAAGGRDNLFHANGFNPIVNWGNRWECTTGEMGGLPDVNTE
NPGFQEYFLNYLNDLIACGADGFRYDTAKHIGVPSDPTDAKSSRNNFWPIATGKESINGK
TLSDADRIFTYGEVLQGDNVPETEYAQYMRMTASSYGYTLRNALSSRNFSVNNLMNWQHA
TPDRLVTWVESHDTYCNAGESAGLTDKQITLGWAVIGARENGTPLFYSRPDGSGPGNRWG
NNVLGARGNDTFMSDEVVAVNKFRNAMVGEDEYLRNANNNSQILQIDRGTVGTCIVNVGG
ATSIDTKTNLDDGTYTDHVSGSTFTVSGGMLKGNIGGESVVVLYTDNAESVSANSTTGSD
SFSGDSLDVELRAKNVTGARYETSEGAEGSYEDGDVITVGSTLDVGESVTVTVSAQGSEG
EISRETVFTKVDRNVAYIDLPSGWDEPYAYVYSEAGGENAAWPGVKMEKVTGEAAEGFTN
LYSYEVPDDIEDPLVIFFGGDNTRRYPADMEDGLPLTGRMVYDDGQWKDMPWTKPEPEDG
PEVTSSVKDGTTFDEESMKVTLSLENAESGTYSLDGGPEQKFTGETTVTVGTGKIADRDI
TLETTATDGETTAEKTFTFHKEFNAEKNGGYLEYGTGTAAKAAKASTQAVPAAANATSAA
LGGKYATNPNGQAGREATITGASDFTADMLIAQGVANDDPRSFRGTHEGPVYDEYALYGA
WDDENVYIGWQYTNVTDVIDPAQGYPISDNGKPYNGDIPQMLLLNLGTGNKATGLMDTGA
YLWDNPIKYETAIDAAIAFSTKPGVGTPALFMADENGTFSYETCVGLAEAGISYKYEDGF
FCGDTLTGIKMNGYEGYVPSMLLDDSSNWVNFLDMGHSTSQDTFYTMTIPMDALGITKDQ
LEENGIGVMHVSTFGAGGIGCTPMDMTMLDAATEPYSKDASTSAEKEDTDIITVPLAQLG
SAEPAPDPGPGPDPEPAEGTLSVNFGADRSSPQADTTDLTLEAEAEGGEGDLSYQFLVDG
KEIQDSDKTTAEWDTVGGDHTISVVVTDEEGHQVTVEKDYSISGEIPDPDPEPAGEIKVS
SFEAALDSPQTQGTSVKFTVNAEGGEGELQYRFYRVAEDSTTTVFRDYAASNVAYCNPPA
AGGYTIYADVKDEAGNTVTTKMSYTWEKNSSDEKLAINDITVNKKSPQTEGTSIQIVVDA
QGKGELQYRFYREKDDNVTVFRDYSTSRSAYCDPAPGSYTIYVDVKDETGKVVTDSIEYK
WIKADNPLTIHSFTASVESPQKHGTSVKLMVDADGGEGTLQYRFYRQGNGITTVFRDYAA
SSTAYCNPPVEGTYILYVDVKDESGVVETYRLLYQWE

Enzyme Prediction     

EC	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	92	378	2.5e-98	0.9887218045112782
CBM74	845	1137	2.2e-95	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	7.90e-151	83	454	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	2.79e-32	84	374	2	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.
COG0366	AmyA	1.40e-22	92	407	26	351	Glycosidase [Carbohydrate transport and metabolism].
cd11320	AmyAc_AmyMalt_CGTase_like	2.44e-22	97	373	49	313	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.
cd11319	AmyAc_euk_AmyA	6.49e-21	93	373	41	297	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDM67953.1	2.09e-310	70	1527	36	1448
AWX97480.1	6.37e-214	81	1243	29	1159
AWX95531.1	6.37e-214	81	1243	29	1159
QQR09576.1	1.05e-145	83	524	33	476
ASB38837.1	1.05e-145	83	524	33	476

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DC0_A	9.23e-96	81	526	3	422	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1BAG_A	3.92e-93	81	526	6	425	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
1UA7_A	9.15e-93	81	526	3	422	ChainA, Alpha-amylase [Bacillus subtilis]
1QHO_A	8.94e-14	67	270	25	232	FIVE-DOMAINALPHA-AMYLASE FROM BACILLUS STEAROTHERMOPHILUS, MALTOSE/ACARBOSE COMPLEX [Geobacillus stearothermophilus],1QHP_A Five-Domain Alpha-Amylase From Bacillus Stearothermophilus, Maltose Complex [Geobacillus stearothermophilus]
4JCL_A	2.79e-11	123	330	77	291	Crystalstructure of Alpha-CGT from Paenibacillus macerans at 1.7 Angstrom resolution [Paenibacillus macerans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P30269	4.42e-108	79	523	143	605	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P00691	5.58e-107	26	704	7	650	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	1.29e-71	77	632	47	567	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
P29750	4.54e-20	86	305	42	258	Alpha-amylase OS=Thermomonospora curvata OX=2020 GN=tam PE=1 SV=1
P27350	1.83e-19	92	524	44	454	Alpha-amylase OS=Streptomyces thermoviolaceus OX=1952 GN=amy PE=3 SV=2

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
0.031302	0.950980	0.015901	0.001184	0.000355	0.000273

TMHMM  Annotations     

start	end
33	55