CAZyme Information: EPE06847.1

Basic Information

• Species: Ophiostoma piceae
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Ophiostoma; Ophiostoma piceae
• CAZyme ID: EPE06847.1
• CAZy Family: GH43
• CAZyme Description: Aamy domain-containing protein [Source:UniProtKB/TrEMBL;Acc:S3C266]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
685	KE148152|CGC1	76023.48	4.5609

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_OpiceaeUAMH11346	8884	1262450	0	8884

• Gene Location: location=KE148152:649698-651755(-)

Full Sequence      

MAYAVDILDRRSSHFVFWLPGLEVSAPPKLLLGTFSENGSKNEFQQLVRQPFVAVDGKPG
LWLLDPNDLQPGLTDGTVYHYWFQLGGLTVTDPIAFTVDYSYLGLENAKARSDSVQPPTV
VKFRDGKLWACDVDGQESARTPIPTQSSLPSNNHMVIYELPTSWARASTQTDRANESGAA
AVKVDVGSFADVTALFDVNARGQHYGSDASHAILQELGINALELLPPADAKPKGDWGYAT
AHYFAPDYDLGTASQLAVLSETINKQGVRMFTDVVMAFGHDSYGDVYGDDTRANVFHLDP
NAEPENPDSYEAGTTGGQKRDGFGGRPWRYIKTVDGYDPESGDGDTTTPKTVQPAWAFHR
AHLTRWMVDFGVGGLRLDSLNNVGSWDFVKSYRERAWALYNQRYGGDADKSKFLIVGEEL
SMPVDMLTGGCLDALWNEKWQQRARAAVLGESWGDDDFEWTVRKLVDCRQDQLNGGSFSD
GSQAVNYLTSHDIEGYRKNRMYDFLADSGVTDTLEIEKRAKLAFVLLLTSVGVPMIFAGE
EFADQQDQSQDMARKQTDPVNYERKNDGGWRQALFTYVALLTKFRTACPALGVDDTNIFH
VDASRGGKVLAWSRGGGTDAAEKPVVVVANFSDQDIVDEYVVPSFPDKDVAGWREVTHDR
DVPAEWIGREPLYAWEAKVYTYWRG

Enzyme Prediction     

No EC number prediction in EPE06847.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	199	549	2.6e-31	0.9498327759197325

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200488	AmyAc_4	2.11e-28	149	591	10	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.
200464	AmyAc_GTHase	1.19e-20	214	546	64	363	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
223373	GlgB	3.22e-17	71	662	80	586	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
200451	AmyAc_family	1.10e-14	214	538	34	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.
273975	pulA_typeI	5.05e-12	130	590	93	531	pullulanase, type I. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family consists of pullulanases related to the subfamilies described in TIGR02102 and TIGR02103 but having a different domain architecture with shorter sequences. Members are called type I pullulanases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDS75203.1|GH0	5.26e-240	6	684	85	743
QDS71939.1|GH0	1.65e-207	6	683	126	765
ANE54330.1|GH0	1.07e-160	5	681	2	669
ATG89000.1|GH0	1.90e-158	5	681	2	669
BAZ11965.1|GH0	9.03e-156	1	681	13	692

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1EHA_A	1.32e-07	214	545	128	422	CRYSTAL STRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
1EH9_A	2.30e-07	214	545	128	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	4.00e-07	214	545	128	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]
2BHU_A	5.50e-07	214	543	153	445	Crystal structure of Deinococcus radiodurans maltooligosyltrehalose trehalohydrolase [Deinococcus radiodurans]
3VGD_A	6.94e-07	214	545	128	422	Ctystal structure of glycosyltrehalose trehalohydrolase (D252E) [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P32818|AMYM_BACAD	4.04e-07	214	632	185	540	Maltogenic alpha-amylase OS=Bacillus acidopullulyticus OX=28030 PE=3 SV=1
sp|O32611|ISOA_FLASP	6.11e-07	201	620	235	679	Isoamylase OS=Flavobacterium sp. OX=239 GN=iam PE=1 SV=1
sp|Q55088|TREZ_SACSO	1.18e-06	214	545	129	423	Malto-oligosyltrehalose trehalohydrolase OS=Saccharolobus solfataricus OX=2287 GN=treZ PE=1 SV=2
sp|Q7NL20|GLGB_GLOVI	7.05e-06	14	314	137	376	1,4-alpha-glucan branching enzyme GlgB OS=Gloeobacter violaceus (strain ATCC 29082 / PCC 7421) OX=251221 GN=glgB PE=3 SV=1
sp|P95867|TREZ_SACS2	8.20e-06	214	545	131	425	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
1.000068	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EPE06847.1.