Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q9P6J3

Entry ID Method Resolution Chain Position Source
AF-Q9P6J3-F1 Predicted AlphaFoldDB

No variants for Q9P6J3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9P6J3

No associated diseases with Q9P6J3

1 regional properties for Q9P6J3

Type Name Position InterPro Accession
domain Glycosyl hydrolase, family 13, catalytic domain 21 - 440 IPR006047

Functions

Description
EC Number 3.2.1.20 Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

7 GO annotations of molecular function

Name Definition
alpha-amylase activity Catalysis of the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more alpha-(1->4)-linked D-glucose units.
dextrin alpha-glucosidase activity Catalysis of the reaction: dextrin + H2O = alpha-D-glucose.
glucan 1,4-alpha-maltotriohydrolase activity Catalysis of the hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotriose residues from the non-reducing chain ends.
maltose alpha-glucosidase activity Catalysis of the reaction: alpha-maltose + H2O = 2 alpha-D-glucose.
oligo-1,6-glucosidase activity Catalysis of the hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose. Releases a free alpha-D-glucose.
starch alpha-glucosidase activity Catalysis of the reaction: starch + H2O = alpha-D-glucose.
sucrose alpha-glucosidase activity Catalysis of the reaction: sucrose + H2O = alpha-D-glucose + beta-D-fructose.

4 GO annotations of biological process

Name Definition
cellular polysaccharide catabolic process The chemical reactions and pathways resulting in the breakdown of polysaccharides, polymers of many (typically more than 10) monosaccharide residues linked glycosidically, as carried out by individual cells.
maltose catabolic process The chemical reactions and pathways resulting in the breakdown of the disaccharide maltose (4-O-alpha-D-glucopyranosyl-D-glucopyranose).
oligosaccharide catabolic process The chemical reactions and pathways resulting in the breakdown of oligosaccharides, molecules with between two and (about) 20 monosaccharide residues connected by glycosidic linkages.
sucrose catabolic process The chemical reactions and pathways resulting in the breakdown of sucrose, the disaccharide fructofuranosyl-glucopyranoside.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKVVPSEKIK PNWWRETSVY QIYPASFKDS NGDGFGDLEG IISKVDYLKA LNVESIWLCP
70 80 90 100 110 120
IYPSPLKDMG YDVSDYKQID SRYGTLEDLD RLMKALHERD MKLVMDLVLN HTSDQHEWFK
130 140 150 160 170 180
ESRSSKTNPK RDWYFWKPAR YNEKGERLPP NNWRSYFDTS AWEWDEATQE YYLHLWSVGQ
190 200 210 220 230 240
PDLNWETPKV REAVHDILRF WLDRGVDGFR LDAINMISKD QRFLDAPITD DRYEYQLAYQ
250 260 270 280 290 300
YYANGPRIHE YLNGIGNILT EYDAFSVGEM PYVLDTNEIL HVVGADRREL TMIFQFDFVD
310 320 330 340 350 360
LDLDPNQHKY IEGSWELSDL KKSLKKWQSA LLSGGGWNAS FIENHDQTRT VSRYLSDSPK
370 380 390 400 410 420
YRAYSSKLMA LFIIFQSGTP FVFQGQELAL ANIPRDWPID EYLDVETQNF WKLFMSGNPS
430 440 450 460 470 480
QEEIEKTMDI VNKRARDNGR TPMHWDSSPN GGFTKAGVKP WMRVTNDYKE WNAANQVNDP
490 500 510 520 530 540
ESPYTFWSKA LELRKELKDA VVYGSFELIS EEDPSIVAFV RESSTYKLII LLNFTGNKVS
550 560 570
YDCPLNLTSY EILLDNYKDF ICMTSPVTLN PYQAVLLKL