CAZyme Information: MGYG000003192_01665

Basic Information

• Species: UBA5416 sp900539175
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA5416; UBA5416 sp900539175
• CAZyme ID: MGYG000003192_01665
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1736		187090.49	4.7868

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003192	4033193	MAG	United States	North America

• Gene Location: Start: 26995; End: 32205 Strand: +

Full Sequence      

MLSMKKTNKNLFSRILALVMALAMILTGVPGTGIPTGAITAEAAVSVAEQNNLTENIQDG
AILHCWCWSFNTIKQNMADIAAAGFTTVQTSPANTCNDTCPNMKIMGNDTEHGTDGCWWW
HYQPTDWKIGNYQLGTRDDFKAMCQEADKYGIKVIVDVIPNHVTPDLDEVSQDLYNAVGG
RNNLFHANGFNEIHQWGNRLECTTGQMGGLPDVNTENPDFQHYFLQYLNDLIECGADGFR
YDTAKHIGVPSDPTDPKSSRNNFWPVATGMESVKGLTLKDKDRVFTYGEVLQGDNVPEAE
YAQYMRMTASSYGGKLRSAVQSKDFSTGNISNWLHATPGRLVTWVESHDTYCNKGESVDL
SKTQIRLAWAVIAARKDGTPLFYSRPNNSNGWSNRWGDNVIGAKGDNEFKSKEVSAVNFF
RNAMAGQSEYLRNPNGNSQILQIDRGTEGTCIVNLGAAASLNNVPTSLADGDYTDQVSGR
TFNVSDGKLSGQLDGEKVAVIYNPSKSGVSATSTSGSDKFSSASLDVKLSAKNVTNATYE
TSEGASGSYTDGTIITVGTTLKEGESVTVTLKAQGEAGAIERTYKFTKVGKNIAYIELPS
GWSEPYCYAYNEAGAENAAWPGVKMEKVSGNTYGYEVPDSVSDPMVIFYGGDNSHRYPAD
MEDGLTLTGSMIYRNGTWDIYRDGPTPTVTPTVTPTVTPTGVPGEGNVAYIELPSGWNEP
YCYAYSKTIAKLENAAWPGVKMEKVSGNLYKYKVPDNISDPLVIFFGGDNSRRYPTDMED
GLALSGNMIYKNGNWSTYSVGPTPTPTVDPGDDLVDGSYDIYIKKPSGWGSNLNCYAYVS
ETLNNGAWPGVSMVSLGSGIYAYNMPEGWTSAKVIFNEGGNQIPGAQQPGMDWTDGTSMI
YKDGSWVKVESKKKLDIVSSLADGSTFDTESETITLTLKNAVSGTYCVDDGPVKDFTDSA
KVVIGQGKIADSNVKVKVTATNGTETKEVTFTYHKKFDAQKNGGYTQYETSVKAAAATAK
AASAAVASAASSESLGGKYATNPNSQKGKYKTISSASDFDESMIIAQGVANDDARTFRGA
HEGPVYDTYALYGAWDDTNLYLGWQFVNVTDVVDPAQGYPISDNGKPWNGDIPQVLALNL
GTGVTSDGSAKGTDDKTGAVNYSDYVWGLPIKYDTAVDALLCFSSKPGVGQPALFRADTD
GYFNYDTAVGFKEGGISFKYEDGFFGSSLYGINANGYQGYKPADLLDASANWTDFLTTNH
SKAQDTFYLMTIPLATLGVSKNDIENNGIGVMHISTFGLSGTACIPMDMTMLDHATEPYS
HDDSTTAEKEDEDRITVPLARLGAGESGLTPTPTPTSTPTPTPIVGTGTMTVNFGADRSS
PQATTTALTLKAIAEGGNGTYTYQFLVDGKEVQNSGKDTYTWSPRSGEHTIGVKVTDGKG
IVTECSKTYVGEGEDPYQPITIKSFTANKQSPQIKGTSIRFAAAAEGGNGTLQYCFYRVL
NGKKTVFRNFAESASAYCNPAAGTYTIGVEVKDADGNTANKEMTYTWSSNETPIVIKSFD
ASKASPQPKGTSVRFSVTAEGGSGALQYRFYRVINGKTTVFRDYASGSAAYCNPAVGTYT
IYVDVKDANGNIATKSMTYTWGSASTELKIKSLTASKVSPQKKGTSVRFAVEAEGGKGDL
QYRFYRVGNGKTTVFRDYSSTKTAYCNPAAGTYIIQVEVKDSEGNTATESMLYQWN

Enzyme Prediction     

EC	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM74	1039	1341	1.3e-105	0.9967948717948718
GH13	68	354	2.3e-97	0.9887218045112782

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	2.97e-146	59	431	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	4.61e-32	60	350	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	6.70e-20	51	295	15	251	Glycosidase [Carbohydrate transport and metabolism].
cd11319	AmyAc_euk_AmyA	1.01e-18	69	349	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.
pfam00128	Alpha-amylase	7.32e-18	122	350	36	290	Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDM67953.1	7.43e-311	4	1733	1	1455
AWX97480.1	1.31e-205	46	1461	18	1166
AWX95531.1	3.52e-205	46	1461	18	1166
QQR09576.1	5.75e-159	59	502	33	476
ASB38837.1	5.75e-159	59	502	33	476

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DC0_A	5.75e-108	56	502	2	420	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1BAG_A	6.96e-106	56	502	5	423	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
1UA7_A	1.62e-105	56	502	2	420	ChainA, Alpha-amylase [Bacillus subtilis]
1VIW_A	2.37e-19	61	492	12	440	TENEBRIOMOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX [Tenebrio molitor]
1CLV_A	3.16e-19	61	492	12	440	YELLOWMEAL WORM ALPHA-AMYLASE IN COMPLEX WITH THE AMARANTH ALPHA-AMYLASE INHIBITOR [Tenebrio molitor],1JAE_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE [Tenebrio molitor],1TMQ_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR [Tenebrio molitor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P30269	5.90e-128	55	853	143	968	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P00691	1.69e-114	41	675	30	650	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	3.55e-82	4	503	1	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
P29750	9.45e-25	21	497	6	467	Alpha-amylase OS=Thermomonospora curvata OX=2020 GN=tam PE=1 SV=1
P08486	7.91e-23	80	502	58	444	Alpha-amylase OS=Streptomyces hygroscopicus OX=1912 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
0.002508	0.996463	0.000260	0.000293	0.000238	0.000224

TMHMM  Annotations     

start	end
12	34