CAZyme Information: MGYG000000104_03075

Basic Information

• Species: Clostridium cuniculi
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium cuniculi
• CAZyme ID: MGYG000000104_03075
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1305		142401.9	4.34

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000104	3679160	Isolate	Canada	North America

• Gene Location: Start: 20898; End: 24815 Strand: -

Full Sequence      

MNNRKKFTSFFIALVFTLSLLFNNFTGLISTTSIAVAATNTSVNQIEDGAILHAWNWSFD
TIKAKLPEIKEAGYTAVQTSPIQGNKEDLMSSTKWWILYQPTNFKIGNAQLGSREEFKSM
CEEADKYGIDIIVDVVANHTGNRGGGTDAYYPANNVDSTIKDNENFWHEHRGVEDWNDRW
QVTHLGIGLPDLNTSNWELQDMVIEFLNDAIACGADGFRFDAAKHIELPSDSGGSDFWPR
VLGSLDRDDLFIYGEVLQGGADNINGYHTYMRTTCDWYGGSVRSAVGYHSTANVNNAKSY
TVSGDPSNLVTWVESHDTYANENMETVALTNEQIKLAWAIIAGRADSTPLFFNRTSGGYL
AGNIGSAGDDMWKDPIVVAANNFRNAMAGEGEYIRTQGNNLFITERGTKGVMIVNVGDST
YVNCDTNLPNGQYTDSVSGNTFTVSNGKLTGNIGSRTIATLGVTEIITKPVVSSSVETGT
KFVDSLNVTLTAKNTTTATYSTNGGTVVTYTNGTTITLGKNANIGDTVTLTLTGKGEDGT
TVTETYEYKKVDKIENSIAKIKLPSGWSSANIYVYDESGSTVKEIAKWPGVAMTDEGNGI
YSYTLPKGWGDNTQVIFNNGSAQIPAAQQAGFSLPTNKIGTYADGNWTLEDIKTEAEVSS
SVADGTEFTDVLNVTLNAKNTTEATYSIDGKEAVTYTDGTTIKLGEDIEAGSTVELTLTG
KNSNGNSVTKTYTYKKADVIVSDTSIAKIKLPSGWTSANIYVYDESGSTVKEIAKWPGVA
MTDEGNGIYSYTLPEGWGDNTQVIFNNGSAQIPAAQQAGFSLPTNKIGTYSDGNWTLEDI
SKPITISSFTSDKSSPQYEETTITLSADATGGSGSLQYKFTATEKTTGEEKVISDYSSKN
SVEWTPLTAGTYEVKVSVKDSNGNVKEESFDFEVKEVFKELQIKSITLDKSQGNLGEAVT
ISTEAEGGSGTLNYKFYYKKDGVYTLIQAYSTSNTVKWTPDESGDYIVYVDVRDGSGTTR
TAYTSYKAYGDSLIIKSFEADKTSVEANTEVTLTVNAEGGTGELSYKFYYKNNDKYTKIQ
DYSTKNSANWTPTEDGYYKLYVDVKDEAENVKTKAFDFIVGNVDDLEMEFTLSTKSGVVN
TPVTIDATSEGGVNPIAYKFYYKKDGTYTMIKDYSDSSSIEWTPEEEGTYVVYVDAKDAS
GKIVSKYINFTVGKGVEITDISLDKTTIKVGDSVNIKTTATGNSNLQYRVAVHDFENTWT
TLHDFKSSNTTTWTPEIADKYVIWVDVIDEDGNYDSKSIEVTVIE

Enzyme Prediction     

No EC number prediction in MGYG000000104_03075.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	57	323	1e-98	0.9924812030075187
CBM26	564	628	1.7e-19	0.84
CBM26	752	816	2.6e-19	0.84

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	5.26e-158	48	394	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	1.51e-41	852	1299	9	470	triple tyrosine motif-containing protein; Provisional
cd11317	AmyAc_bac_euk_AmyA	3.63e-32	49	265	2	182	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	5.23e-32	891	1303	139	569	triple tyrosine motif-containing protein; Provisional
PRK14081	PRK14081	9.79e-31	842	1197	287	648	triple tyrosine motif-containing protein; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDM67953.1	1.49e-223	37	1293	36	1447
AWB44629.1	3.65e-211	35	638	26	648
APB71173.2	1.15e-210	37	690	50	703
AET60999.1	1.21e-210	36	677	41	682
ASR47410.1	1.36e-210	38	638	43	644

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DC0_A	1.04e-105	45	461	2	419	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1UA7_A	9.96e-104	45	461	2	419	ChainA, Alpha-amylase [Bacillus subtilis]
1BAG_A	1.47e-102	45	461	5	422	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
1JD7_A	1.89e-18	52	454	8	434	ChainA, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]
1G94_A	4.29e-18	52	454	8	434	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	2.66e-134	45	644	46	650	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	6.60e-105	47	458	52	457	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	3.06e-75	44	809	143	880	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P22630	1.81e-26	51	418	24	413	Alpha-amylase OS=Aeromonas hydrophila OX=644 PE=3 SV=1
P09107	3.41e-22	50	451	28	457	Alpha-amylase (Fragment) OS=Tribolium castaneum OX=7070 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
0.003497	0.995056	0.000653	0.000310	0.000217	0.000204

TMHMM  Annotations     

start	end
7	29