CAZyme Information: MGYG000004520_00798

Basic Information

• Species: Ruminococcus_E bromii_A
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E bromii_A
• CAZyme ID: MGYG000004520_00798
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
998	MGYG000004520_8|CGC1	107657.53	4.2654

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004520	2155170	MAG	Israel	Asia

• Gene Location: Start: 15648; End: 18644 Strand: +

Full Sequence      

MKKRITSIVLSACMLLSCVAVGSFSTQAAEVTSPEAVSSGSQEPLDHIQGANILHCFDWS
YNSIKANLKDIKDAGYTAVQTSPVQAPKDYSASYKKQSDEWWKLYQPISFNIADGNTWLG
TKAELKELCTEAENYGIKVIVDIVANHMADVDSSGNTRGNISSQIEAEVRNNDSNWHLNS
SWANSDNDRYSMTQGSIGQPDVNTGSSYIQNRVKNLLIDCINQGVDGFRFDTAKHIELPT
DSGFGSQFWPTVVNGSQSSTSNKIFYYGEVLNGCATDISNYTKYLSVTDNYSGDTKLYAA
NTGNAQGLANSNYAKGAGANKTVLWAESHDTYMGGTGSGGYQNTKSVPDSSIVKAWAMVG
SRADASSLFFARPAANMGDASTDTTWKSKAVAEVNKFKNYFDGESEYLSSSGSVAYNERG
TSGVVIAKLDGAGSVNISAKRMKDGTYTDQVTGNEFKVSNGNISGTVGSTGVAVVYNAVT
PGPSVSAVPGTSSYKTDTLTITLNYKNGATSGWYSIDGSDYKSFTNGEKITIGAGVAYGT
STILNVKASDGTTTSDPISYKYTKVDPSAVQKIYFDNSSYNWSSVYAYIYSDETTKNASW
PGEKMTLDSSTGYYSIEVPENLADGYVIFTESNNATTNRYPADMQPGLSLGGKNMLFKAN
NEWVEYNVVRPTEATEATTSTTPSTATEPTTMTPTIRVLIGDVDNDGIVSIKDATIIQRY
INGVNTINDTEEFKLAADTNGDGSIDILDVTVIQYYLANNRAMAGNCGQYTGGENPTTPS
TPETEPTEPTEPTETQPGNNYVYFKNTSNWSSVMAYYWSEEDITLTSWPGVAMTSVGDNV
YRVEVPSTATNIIFNNGGSDQTGDIALQGYGKIYENGSWSNYNGSSEQPTSPETSTNPDS
GDNYTITFTNNRNWGNVNCYYWSEADTTMTAWPGTQMTYSTTNDFGEKIYTIEIPSSADR
MIFNDGSGSQTVDIAVTGSAKYYISGGSGSACTVETWE

Enzyme Prediction     

No EC number prediction in MGYG000004520_00798.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	59	334	5.8e-81	0.9849624060150376
CBM26	802	864	9.7e-19	0.88

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	1.08e-102	53	408	4	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	1.58e-29	53	339	4	246	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	2.42e-20	59	269	26	238	Glycosidase [Carbohydrate transport and metabolism].
pfam16738	CBM26	3.66e-17	802	865	1	67	Starch-binding module 26. CBM26 is a carbohydrate-binding module that binds starch.
smart00642	Aamy	7.35e-16	53	150	3	97	Alpha-amylase domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCT06294.1	3.70e-185	2	732	4	743
APB71173.2	3.52e-108	53	656	65	654
QDY86356.1	5.53e-108	53	656	57	646
QYK62214.1	6.85e-108	53	656	65	654
ASR47410.1	1.08e-107	53	656	57	646

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UA7_A	2.84e-78	48	476	3	420	ChainA, Alpha-amylase [Bacillus subtilis]
1BAG_A	8.20e-78	48	476	6	423	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
3DC0_A	2.76e-77	48	476	3	420	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1G94_A	3.96e-18	54	339	6	273	CRYSTALSTRUCTURE ANALYSIS OF THE TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS IN COMPLEX WITH A HEPTA-SACCHARIDE AND A TRIS MOLECULE [Pseudoalteromonas haloplanktis],1G9H_A TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA-AMYLASE, COMII (PSEUDO TRI-SACCHARIDE FROM BAYER) AND TRIS (2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL) [Pseudoalteromonas haloplanktis],1L0P_A Crystal Structure Analysis Of The Complex Between Psychrophilic Alpha Amylase From Pseudoalteromonas Haloplanctis And Nitrate [Pseudoalteromonas haloplanktis]
1JD7_A	4.11e-18	54	339	6	273	ChainA, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	2.24e-96	33	647	32	639	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	4.66e-64	38	504	41	490	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	3.90e-50	46	618	143	752	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P41131	1.18e-18	53	241	28	207	Alpha-amylase OS=Aeromonas hydrophila OX=644 GN=amyA PE=3 SV=1
O18345	3.99e-18	51	348	29	324	Alpha-amylase 2 OS=Drosophila ananassae OX=7217 GN=Amy58 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
0.000744	0.793081	0.205122	0.000523	0.000278	0.000220

TMHMM  Annotations     

start	end
7	29