CAZyme Information: MGYG000001725_02407

Basic Information

• Species: Massilimaliae sp900752435
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Massilimaliae; Massilimaliae sp900752435
• CAZyme ID: MGYG000001725_02407
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1166	MGYG000001725_27|CGC1	124277.38	6.0802

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001725	2564044	MAG	Sweden	Europe

• Gene Location: Start: 10221; End: 13721 Strand: -

Full Sequence      

MNQSKKRFISISLSVLMAFTTMLSSAGTVFAEETEIDTSAVTTTETTNNEANPYGLASKT
KDGVILHAFCWNFNTIKANLKDIAAAGYTTVQTSPINRCFDEDQGPQLFGNGKWYYHYQP
TEWTIGNYQLGTRDEYKALCAEAEKYGIKIISDVLPNHTTPTTSNIKGQLKSLMDSGKLY
HQNGWNDISYDSRWSIITGKMGGLPDVNTEGYDFQKYYMEFVNDVVACGGDGFRYDTAKH
IGTPIDPTDNADHPNGNNFWPLVTGKQSYSGIPSLSNPSSQFIYGEILQGDENKEGTPYA
EYAKYLDGMTASKYGILPPDDTGWRGVLGTALTNKDFSTSNLVGWAHPLNNGDKMVSWVE
SHDTYCNDHVSAGYSDWQIRMGWAVIAARSEGTPLFFNRPANSSSGNVWGDNLIGKAGND
EWKSTEVAAVNRFRNAMIGEKDYMRNPDNNKQILQIDRGTKGTCIINLGGSTSINNTTTM
ADGQYKDQVSGRIFTVSGGRISGQLDGGKIAVIYNAEPIEDYSISASPDSGSYKTDTQRV
TISTENVSNAQYRIDSGSWTSFSGSTTVTIGSASDAYGTKHTLYVQGTDKNGQTVSETFT
YTKVDPDAANIAYMKKPSSWANAYCYVYNENPDPTVSVQENAPWPGVAMTSVGNGIYSYE
VPDYDNPRVIFTNGVKDGTLKYPADDTPGVDAAGLEIEGSMIWDGASSWEPYTQDVAVTG
VTMSPTSLSLKVGETGSLTATVAPSNATDKTLTWKSSNTSVATVSDGTVTAKAVGTATIT
ATSNNGKTATATVTVTKDDVAVTSVSVSPASLSLTVGDTGELTATVSPSNATDKTLTWKS
SNTSVATVNNGTVTAKAAGTATITATSNNGKVGTATVKVTNPVSTLKVSNFSTNKGTSAV
TGTQVMLMASAEGGTGSYQYAFSVCNSEGKWYKIQAASAKNTAVWNASPAGQKTLYAYVK
DSSGKVEQKTINFTVTDGKPLAVSSFTTNKGTSAVSGTQVTLTATGAGGTGGYQYAFSVC
NSEGKWYKIQAASAKNTAVWNASPAGQKTLYAYVKDSSGKVEQKTINFTVTDSKPLTVSS
FTTNKGTSATKGTKVTLTATASGGTGSYQYAFSVCNSEGKWYKIQAASAKNTAVWDATPA
GQKTLYAYIKDASGKVEQKTINFTVK

Enzyme Prediction     

EC	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	71	369	2.9e-85	0.9924812030075187
CBM26	613	675	6.3e-16	0.7866666666666666

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	7.66e-133	62	444	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.
COG5492	YjdB	8.63e-21	656	874	110	328	Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction only].
cd11317	AmyAc_bac_euk_AmyA	9.77e-18	63	364	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.
pfam16738	CBM26	3.11e-17	613	674	2	59	Starch-binding module 26. CBM26 is a carbohydrate-binding module that binds starch.
pfam02368	Big_2	3.47e-16	719	786	1	69	Bacterial Ig-like domain (group 2). This family consists of bacterial domains with an Ig-like fold. Members of this family are found in bacterial and phage surface proteins such as intimins.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDM67894.1	4.31e-151	52	1166	42	1038
QHB63346.1	2.14e-143	23	775	35	780
AJE06459.1	2.33e-143	23	775	38	783
AII76764.1	3.32e-143	23	775	35	780
AMK57570.1	5.93e-141	54	776	74	791

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UA7_A	2.36e-97	61	514	4	420	ChainA, Alpha-amylase [Bacillus subtilis]
3DC0_A	3.27e-97	61	514	4	420	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1BAG_A	3.59e-97	57	514	3	423	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
1QHO_A	2.46e-13	46	397	25	360	FIVE-DOMAINALPHA-AMYLASE FROM BACILLUS STEAROTHERMOPHILUS, MALTOSE/ACARBOSE COMPLEX [Geobacillus stearothermophilus],1QHP_A Five-Domain Alpha-Amylase From Bacillus Stearothermophilus, Maltose Complex [Geobacillus stearothermophilus]
1JD9_A	2.88e-11	66	412	6	364	ChainA, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	8.77e-119	47	691	35	641	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P30269	7.57e-111	62	513	147	605	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P23671	6.38e-74	56	515	47	462	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
P27350	1.93e-13	60	515	34	455	Alpha-amylase OS=Streptomyces thermoviolaceus OX=1952 GN=amy PE=3 SV=2
P19531	1.40e-12	46	397	58	393	Maltogenic alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyM PE=1 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
0.000988	0.997910	0.000310	0.000333	0.000233	0.000206

TMHMM  Annotations     

start	end
9	31