CAZyme Information: TSTA_101220-t26_1-p1

Basic Information

• Species: Talaromyces stipitatus
• Lineage: Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces stipitatus
• CAZyme ID: TSTA_101220-t26_1-p1
• CAZy Family: GH72
• CAZyme Description: maltase MalT

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
587		67718.31	5.3066

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TstipitatusATCC10500	12629	441959	146	12483

• Gene Location: location=EQ962658:1115695-1117557(-)

Full Sequence      

MSPSAIETVPTGTNNWWKEATIYQVYPASFKDSNGDGWGDILGVIEKVPYLHSLGVDVVW
LSPMYDSPMHDMGYDISDYENVLPAYGTVADIEKLIDECHKHGMRLILDLVVNHTSDQHK
WFQESRSSKGNPKRDWYFWRPPRYDAYGNRMPPTNYRGYFAGSTWTWDEHTQEYYLHLYA
KEQPDLNWDNEVTRKAIYDSAIRFWLDKGVDGFRVDTVNKYSKHTDFPDAPITDPKSFIQ
PAIGMWCNGPRIHEFLREMYDEALEPYGDVVTVGELANTPDPAHVLKYVSAAEKQLSMVF
HLDIGHIGMGHSLEDKYILQPWELTEMKSIVNKWQTFIEGTDGWTTAFCENHDNGRSVSR
FASDAPEFREVSAKMLALMMVAMTGTLSIYQGQEIGMINAPREWSIDEYKDIEGLGYYRE
AQNQVASGVDPTREKRIMDGLRILARDHARLPMQWDDSPEAGFTTGKPWMRTHDLYRDIN
VKKQEADPDSVLSFWKKVLRLRKDYRQLFIHGKFEVLDFENLETFCFVKSRGEKRALVVL
NFTGIEQPCSQAEMAAGMKLLASNYSECSSSQRLRPYEGRIYVSDKS

Enzyme Prediction     

EC	3.2.1.10:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	39	399	2e-170	0.9944289693593314

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200472	AmyAc_SI_OligoGlu_DGase	0.0	18	504	1	428	Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins. The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. 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 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.
274115	trehalose_treC	0.0	16	582	1	541	alpha,alpha-phosphotrehalase. Trehalose is a glucose disaccharide that serves in many biological systems as a compatible solute for protection against hyperosmotic and thermal stress. This family describes trehalose-6-phosphate hydrolase, product of the treC (or treA) gene, which is often found together with a trehalose uptake transporter and a trehalose operon repressor.
182849	PRK10933	1.17e-170	15	585	6	551	trehalose-6-phosphate hydrolase; Provisional
200470	AmyAc_OligoGlu_like	3.66e-145	16	508	2	446	Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. 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.
200469	AmyAc_OligoGlu	1.06e-144	15	521	1	469	Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBF75992.1|GH13_40	0.0	1	583	1	582
QMW36030.1|GH13_40	0.0	1	584	1	583
QRD93014.1|GH13_40	0.0	1	584	1	583
BAE65599.1|GH13_40	0.0	1	584	1	583
UDD65242.1|GH13_40	0.0	1	584	1	583

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7P01_A	5.19e-203	16	582	16	578	Chain A, BaAG2 [Blastobotrys adeninivorans],7P01_B Chain B, BaAG2 [Blastobotrys adeninivorans],7P07_A Chain A, BaAG2 [Blastobotrys adeninivorans],7P07_B Chain B, BaAG2 [Blastobotrys adeninivorans]
3A47_A	5.61e-188	1	585	3	589	Crystal structure of isomaltase from Saccharomyces cerevisiae [Saccharomyces cerevisiae],3A4A_A Crystal structure of isomaltase from Saccharomyces cerevisiae [Saccharomyces cerevisiae],3AJ7_A Crystal Structure of isomaltase from Saccharomyces cerevisiae [Saccharomyces cerevisiae]
3AXH_A	4.53e-187	1	585	3	589	Crystal structure of isomaltase in complex with isomaltose [Saccharomyces cerevisiae],3AXI_A Crystal structure of isomaltase in complex with maltose [Saccharomyces cerevisiae]
4M8U_A	3.38e-166	14	584	2	559	The Structure of MalL mutant enzyme V200A from Bacillus subtilus [Bacillus subtilis subsp. subtilis str. 168]
4MAZ_A	1.98e-165	14	584	2	560	The Structure of MalL mutant enzyme V200S from Bacillus subtilus [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q02751|MALT_CANAX	7.46e-216	14	585	4	570	Alpha-glucosidase OS=Candida albicans OX=5476 GN=MAL2 PE=1 SV=4
sp|Q08295|IMA2_YEAST	8.89e-189	1	585	3	589	Oligo-1,6-glucosidase IMA2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=IMA2 PE=2 SV=1
sp|P38158|MAL32_YEAST	1.06e-188	10	583	7	582	Alpha-glucosidase MAL32 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=MAL32 PE=1 SV=1
sp|P53341|MAL12_YEAST	1.06e-188	10	583	7	582	Alpha-glucosidase MAL12 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=MAL12 PE=1 SV=1
sp|P07265|MAL62_YEASX	1.22e-187	10	583	7	582	Alpha-glucosidase MAL62 OS=Saccharomyces cerevisiae OX=4932 GN=MAL62 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000040	0.000022

TMHMM  Annotations     

There is no transmembrane helices in TSTA_101220-t26_1-p1.