CAZyme Information: FOXG_04689-t26_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOXG_04689-t26_1-p1
• CAZy Family: CBM21
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
785	CM000592.1|CGC10	84674.24	7.1403

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Foxysporum4287	21354	426428	429	20925

• Gene Location: location=CM000592.1:5207091-5209639(-)

Full Sequence      

MRFLPSTLFVWLLLTIKILAAPSNSAHEKRATQVSLKSYTYTGSTLAGSVKIQNIAYAKA
VSVYWAAGSTWMSTPISASYSTGPDSSGYETWTFSGTAASATQFYIAYIVSGTTYYDPGN
NVNYQITSSTSKTSTSTTGTSTRASSTITSSTTSSSTVPAGTGGTVSPSSIPPFYSATIP
TEAAATAPTGCGNFNGKDSCASGSTYTVPDSAENRRWQTPPKGDTAYFDTFQSYRSLTGY
ADIQYSSSKTSAAVVINCLSRTDETLTYSFNGANQTSNVYQANQSTKGGLTIVVYGSSGS
VLTLDPLYFLWENAVISGQQSSFSDGQKGAIVELFGWPYTDIAKECSFLSKAGYMGLKIW
PPQEHVWGSNYYEPDNQFRPWYFVYQPVSYRLQSRLGSRAELRAMIQTCRAVGVRVYFDA
VLNHMSGNGNDVQNHRNTDCSLYTGHNGTAGSPFYTWGQTYLINPFSGTRPTVEFPAVPY
GPTDFHCERSLSSWTDGQVITKGWLVGLTDLNSEKPYVQDRVATYLVDVLSLGASGFRVD
AAKHIGPAMMAQIYKRVKQKLGGGDFPADFISWNEVILGGEKDLLACGGGEWSWYTNFDN
VLSAAGLSSTDIAKIKIWSSDYPKEFPACGSWVIPASRFAIQNDDHDQQSPGSSSRDMGD
SGSVLIKDKDISKHRAFEVQLFSRTDGDWKIKLVLSSYMFASNGASGFPDGKSDCSLYTG
SQSQSGCLGMAYDQAYVASACGYGGGTLMAGKYTRVHRDLSIINAMRAWVGLGSTTALAL
GISGC

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	353	583	7.5e-49	0.6802973977695167

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200456	AmyAc_bac_euk_AmyA	1.80e-126	328	772	1	329	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.
200454	AmyAc_bac1_AmyA	4.31e-37	329	565	2	202	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.
214758	Aamy	9.69e-19	331	429	3	99	Alpha-amylase domain.
200491	AmyAc_bac_CMD_like	7.10e-12	390	589	67	217	Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. 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.
395077	Alpha-amylase	8.46e-11	348	546	27	178	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
EGX42980.1|CBM21|GH13	0.0	29	785	37	789
QRW16798.1|CBM21|GH13	8.94e-254	32	785	33	783
QRV88491.1|CBM21|GH13	7.03e-250	25	782	66	839
QRV73700.1|CBM21|GH13	2.95e-246	32	782	77	839
QRW02641.1|CBM21|GH13	2.95e-246	32	782	77	839

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1PIF_A	1.76e-39	330	707	12	351	PIG ALPHA-AMYLASE [Sus scrofa],1PIG_A PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE OLIGOSACCHARIDE V-1532 [Sus scrofa],4X0N_A Porcine pancreatic alpha-amylase in complex with helianthamide, a novel proteinaceous inhibitor [Sus scrofa]
1PPI_A	2.39e-39	330	707	12	351	THE ACTIVE CENTER OF A MAMMALIAN ALPHA-AMYLASE. THE STRUCTURE OF THE COMPLEX OF A PANCREATIC ALPHA-AMYLASE WITH A CARBOHYDRATE INHIBITOR REFINED TO 2.2 ANGSTROMS RESOLUTION [Sus scrofa]
1JFH_A	3.23e-39	330	707	12	351	STRUCTURE OF A PANCREATIC ALPHA-AMYLASE BOUND TO A SUBSTRATE ANALOGUE AT 2.03 ANGSTROM RESOLUTION [Sus scrofa]
1KXQ_A	4.37e-39	330	707	12	351	Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXQ_B Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXQ_C Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXQ_D Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXT_A Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXT_C Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXT_E Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXV_A Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXV_B Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa]
1BVN_P	4.37e-39	331	707	13	351	Pig Pancreatic Alpha-Amylase In Complex With The Proteinaceous Inhibitor Tendamistat [Sus scrofa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P00688|AMYP_MOUSE	6.31e-41	301	712	4	364	Pancreatic alpha-amylase OS=Mus musculus OX=10090 GN=Amy2 PE=1 SV=2
sp|P09107|AMY_TRICA	2.87e-40	328	581	26	247	Alpha-amylase (Fragment) OS=Tribolium castaneum OX=7070 PE=3 SV=2
sp|O97396|AMY_PHACE	1.23e-39	304	653	3	311	Alpha-amylase OS=Phaedon cochleariae OX=80249 PE=2 SV=1
sp|P19961|AMY2B_HUMAN	6.26e-39	302	649	5	317	Alpha-amylase 2B OS=Homo sapiens OX=9606 GN=AMY2B PE=1 SV=1
sp|Q9BN01|AMYB_DROYA	1.19e-38	314	558	14	222	Alpha-amylase B OS=Drosophila yakuba OX=7245 GN=Amy-d PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000221	0.999760	CS pos: 20-21. Pr: 0.9774

TMHMM  Annotations     

There is no transmembrane helices in FOXG_04689-t26_1-p1.