CAZyme Information: Z517_06960-t43_1-p1

Basic Information

• Species: Fonsecaea pedrosoi
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Fonsecaea; Fonsecaea pedrosoi
• CAZyme ID: Z517_06960-t43_1-p1
• CAZy Family: GH32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
681	KN846972|CGC23	76307.61	5.6186

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FpedrosoiCBS271-37	12573	1442368	46	12527

• Gene Location: location=KN846972:3208074-3210119(-)

Full Sequence      

MAPIFDLLQRRKERFVLWSPASQSVPRLILGTFKATPSPGAVTTLFAGDLSQTQNGLWEL
APDTIQPPLQNDKVYHYWFEVDNTYPTSTGSGKIKITDPLAYTVDYKQFGDQPRVASMQP
PAVIKFRDGKLWPCDIDGTEVERVPDPVQSQVPPNNQMVIYELPASWAKSGPNGKQIDRG
TFADVQALFDKATPGVRFSSISAVRKEAIVADLGINALELLPIADSKYQDQWGYSTAHYF
APDADLGSTASLVDLIQTITPSTRLILDTVMAFGHDPYIYAAFMQFHLVALDPDHPNDPL
QKFTESGNADSYTSHNQGPRNPYGGSLWRYIKDPQQTYDPQTGQATLKHPPSWSFHRAHL
HRWLLDFGVSGLRLDSINNVANYNFIKYYKDYAWQLHQTRGGSTNKFIVIGEELSVPKDL
LTSGTLNALWNEPFQGRIRAAIVGEAADGDNFEWTVRKMVDCTLDGYTDGAQAVNYITSH
DVEGNRKERLYNFLSNCRVDDIERRAKLAFACFLTAVGIPMIFAGEEFCDQMDLDISEKQ
SDPVNYERKSDDWRTRVFNYVATLVDLRKNCPALGVDDTSFIHVDQSRGGKIMAWVRGTT
NPVVVVANFTDQDTPGAQYVVPNWPDRDRNDWREITQNRAVPAAWVGKEPLMHWEAKVYT
CWKAGAVNGQTNGVNGTHSSG

Enzyme Prediction     

No EC number prediction in Z517_06960-t43_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	210	528	6.6e-30	0.8762541806020067

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200488	AmyAc_4	2.23e-35	151	574	9	386	Alpha amylase catalytic domain found in an uncharacterized protein family. 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 (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.
223373	GlgB	5.26e-23	14	636	39	581	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
200464	AmyAc_GTHase	5.76e-21	153	528	33	359	Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called Maltooligosyl trehalose Trehalohydrolase). Glycosyltrehalose trehalohydrolase (GTHase) was discovered as part of a coupled system for the production of trehalose from soluble starch. In the first half of the reaction, glycosyltrehalose synthase (GTSase), an intramolecular glycosyl transferase, converts the glycosidic bond between the last two glucose residues of amylose from an alpha-1,4 bond to an alpha-1,1 bond, making a non-reducing glycosyl trehaloside. In the second half of the reaction, GTHase cleaves the alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose and malto-oligosaccharide. Like isoamylase and other glycosidases that recognize branched oligosaccharides, GTHase contains an N-terminal extension and does not have the conserved calcium ion present in other alpha amylase family enzymes. 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. Glycosyltrehalose Trehalohydrolase Maltooligosyltrehalose Trehalohydrolase
200451	AmyAc_family	2.97e-18	159	524	1	253	Alpha amylase catalytic domain family. 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; and 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 this 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.
224440	PulA	1.62e-17	154	574	168	591	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDS75203.1|GH0	2.36e-255	2	666	81	746
QDS71939.1|GH0	2.16e-220	5	662	125	765
ANE54330.1|GH0	4.60e-170	6	659	3	668
ATG89000.1|GH0	1.30e-169	6	659	3	668
BAY26937.1|GH0	8.40e-166	4	660	2	664

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1EHA_A	9.01e-10	193	531	113	422	CRYSTAL STRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
1EH9_A	1.19e-09	193	531	113	422	Crystal Structure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGG_A	1.19e-09	193	531	113	422	Crystal structure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltoheptaose [Saccharolobus solfataricus],3VGH_A Crystal structure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]
3VGD_A	3.60e-09	193	531	113	422	Ctystal structure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]
3VGE_A	6.26e-09	193	531	113	422	Crystal structure of glycosyltrehalose trehalohydrolase (D252S) [Saccharolobus solfataricus],3VGF_A Crystal structure of glycosyltrehalose trehalohydrolase (D252S) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q55088|TREZ_SACSO	6.13e-09	193	531	114	423	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
sp|Q825Q8|GLGB2_STRAW	1.11e-08	128	283	56	220	1,4-alpha-glucan branching enzyme GlgB 2 OS=Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) OX=227882 GN=glgB2 PE=3 SV=1
sp|Q8XT76|GLGB_RALSO	1.70e-08	154	635	287	728	1,4-alpha-glucan branching enzyme GlgB OS=Ralstonia solanacearum (strain GMI1000) OX=267608 GN=glgB PE=3 SV=1
sp|Q82JF0|GLGB1_STRAW	5.28e-08	128	283	295	459	1,4-alpha-glucan branching enzyme GlgB 1 OS=Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) OX=227882 GN=glgB1 PE=3 SV=1
sp|P95867|TREZ_SACS2	2.96e-07	204	543	125	437	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=treZ PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000066	0.000000

TMHMM  Annotations     

There is no transmembrane helices in Z517_06960-t43_1-p1.