CAZyme Information: MGYG000000977_00788

Basic Information

• Species: Clostridium sp900539375
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp900539375
• CAZyme ID: MGYG000000977_00788
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1316	MGYG000000977_6|CGC2	140977.75	9.3201

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000977	2927434	MAG	Australia	Oceania

• Gene Location: Start: 51789; End: 55739 Strand: -

Full Sequence      

MGKTRKRLTSIVATLAVTSSLFVGSFSTNASAATVSTNNESTYASEKAATQADSIKDGVI
LHAWNWSFNSIKENMKEIADAGYTSIQTSPAQACRKGSGWNNADKTNTNSNPSWYWLYQP
TYFTLGNEYLGTVAEFKAMCTEAHKYGVKIIVDVVANHLADGANASNADATLYNEARKSP
RINHWNVRSEVTQGCCIGMPDINTASLSSQKIIGDYLVECLNAGADGFRFDAAKSIELPA
SEEGNNPSSDFWPNIINRVKSVKSDAFIYGEVLQGDEPGTNFNNYTKYMSVTASTYGWHL
RSAVGYEMWQEEKNGVDVLGCNGNNGKVDPHTDTLATTQYAAGNGETPGSITNDKLVGWV
ESHDLYANAGATRGMTQIQREMAWAMLAGRAKIVPLFFNRPTDRSFGDNPMNPQGEAYNT
MGQRGSDDFASKNVMAVNLFHNAMASEGEKISSINNDKVFKIERGNKGILLTNVGGSTSI
STSTSLPNGTYENQAASGGTFTVSNGTLTGNMEGSSIAVLYVGATSGGGSTGGGGSTGGG
GSTGGGGSTVISGAASAYFVKPSGWGTPNAYVYTKSGSSVTELNGEWPGKAMKDEGNGVY
SYTLPEGTSSALIIFNDGSNQIPGAQQSGYAITSSKSMKYENGTWSETVVDTSLKVKEIT
TDLQSPQSTDTDIKITANASGQGTIQYKFTVTKGSTSETLSSFSTKNTVTWTPSEAGTYT
IKVEAKNDKGETAELTKQFVIKTGDVDSDAPVIKSIKVNKTAPQPKNSSITFTVNAIGGE
NVGNGLLFYKFFVTEPNGKEQVVQYYSRKNTYTLKATKEGTYKVRVEVQNADNTTVSKEM
SYEIATVVTPTELTLNSFTSSKSSPQQLGTSIVLSADAEGGTGSLTYKYYVKFNGSTTTL
STTTSNTYTWKPTKAGTYTVYVDVTDEDGNKVSDNFSYTIKSNEADNLVINSFTASKQSP
QVSGTQVKLTAKATGTGTLQYKFLIKDASGNWAVLRDYGKSNTYIWRTGKAGNKTLYVDV
KDSNGKVTRASMSYTVKAAAPKVTSFTADKKSPQVSGTQVKLTAKATGTGTLQYKFLIKD
ASGNWAVLRDYGKSNTYIWRTGKAGNKTLYVDVKDSNGKVTRASMSYTVKAAAPKVTSFT
ADKKSPQASGTQLLLMAQATGEGELQYKFLVKDASGNWFVIQDYSSSNIAVWKASKTGNK
TLYVDVKDSNGQVTRKSMSYTITAAAPTVTSFTADKKSPQASGTQLLLMAQATGEGELQY
KFLVKDASGNWFVIQDYSSSNIAIWKAGKTGNKTLYVDVKDSNGKVTRKSISYTIK

Enzyme Prediction     

No EC number prediction in MGYG000000977_00788.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	66	369	3.4e-82	0.9887218045112782
CBM26	558	626	1.6e-21	0.8933333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	4.97e-113	57	451	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.
PRK14081	PRK14081	1.01e-34	861	1301	9	458	triple tyrosine motif-containing protein; Provisional
PRK14081	PRK14081	9.82e-34	662	1115	9	458	triple tyrosine motif-containing protein; Provisional
cd11317	AmyAc_bac_euk_AmyA	8.53e-33	58	376	2	249	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.
PRK14081	PRK14081	6.38e-32	956	1315	9	377	triple tyrosine motif-containing protein; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDM67894.1	9.87e-138	1	1136	1	1044
CDM67953.1	5.10e-132	1	1222	1	1457
CDM70432.1	9.08e-111	1	647	1	741
QGG57929.1	9.78e-109	56	633	54	596
ASR47410.1	3.65e-108	56	639	53	647

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DC0_A	4.70e-98	54	521	2	420	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1BAG_A	7.12e-98	52	521	3	423	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
1UA7_A	4.48e-97	54	521	2	420	ChainA, Alpha-amylase [Bacillus subtilis]
5A2A_A	2.54e-11	71	276	46	224	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	2.91e-11	71	276	80	258	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	7.76e-106	30	630	31	640	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	6.34e-78	42	521	39	461	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
P30269	1.77e-58	53	520	143	605	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P41131	1.29e-18	57	297	25	251	Alpha-amylase OS=Aeromonas hydrophila OX=644 GN=amyA PE=3 SV=1
P29750	2.45e-15	48	524	27	484	Alpha-amylase OS=Thermomonospora curvata OX=2020 GN=tam 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
0.000433	0.998689	0.000186	0.000278	0.000194	0.000163

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000977_00788.