y
Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 894626 |
Family | GH31 |
Protein Properties | Length: 917 Molecular Weight: 102424 Isoelectric Point: 6.9451 |
Chromosome | Chromosome/Scaffold: 6 Start: 12441944 End: 12442456 |
Description | |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH31 | 264 | 756 | 0 |
FYFIAGPSPLNVVDQYTQLIGRPAPMPYWSLGFHQCRWGYHNLSVVEDVVDNYKKAKIPLDVIWNDDDHMDGHKDFTLNPVAYPRAKLLAFLDKIHKIGM KYIVINDPGIGVNASYGTYQRAMAADVFIKYEGKPFLAQVWPGPVYFPDFLNPKTVSWWGDEIKRFHDLVPIDGLWIDMNEVSNFCSGLCTIPQGKQCPS GEGPGWVCCLDCKNITKTRWDDPPYKINATGVVAPVGFKTIATSATHYNGVREYDAHSIYGFSETIATHKGLLDVKGKRPFILSRSTFVGSGKYAAHWTG DNQGTWQSLQVSISTMLNFGIFGVPMVGSDICGFYPQPTEELCNRWIEVGAFYPFSRDHANYYSPRQELYQWDTVADSARNALGMRYKILPFLYTLNYEA HMSGAPIARPLFFSFPEYTECYGNSRQFLLGSSLMISPVLEQGKTEVEALFPPGSWYHMFDMTQAVVSKNGKRVTLPAPLNFVNVHLYQNTIL |
Full Sequence |
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Protein Sequence Length: 917 Download |
MASSCSSSLA FSLSLLLALI LCFTPTQSSK TIGKGYRLIS IEESPDGGFI GYLQVKQKNK 60 IYGSDITTLR LFVKHETDSR LRVHITDAKQ QRWEVPYNLL PREQPPQVGK VIGKSRKSPI 120 TVQEISGSEL IFSYTTDPFT FAVKRRSNHE TLFNTSSSLV FKDQYLEIST SLPKEASLYG 180 LGENSQANGI KLVPNEPYTL YTEDVSAINL NTDLYGSHPM YMDLRNVGGK AYAHAVLLLN 240 SNGMDVFYRG DSLTYKVIGG VFDFYFIAGP SPLNVVDQYT QLIGRPAPMP YWSLGFHQCR 300 WGYHNLSVVE DVVDNYKKAK IPLDVIWNDD DHMDGHKDFT LNPVAYPRAK LLAFLDKIHK 360 IGMKYIVIND PGIGVNASYG TYQRAMAADV FIKYEGKPFL AQVWPGPVYF PDFLNPKTVS 420 WWGDEIKRFH DLVPIDGLWI DMNEVSNFCS GLCTIPQGKQ CPSGEGPGWV CCLDCKNITK 480 TRWDDPPYKI NATGVVAPVG FKTIATSATH YNGVREYDAH SIYGFSETIA THKGLLDVKG 540 KRPFILSRST FVGSGKYAAH WTGDNQGTWQ SLQVSISTML NFGIFGVPMV GSDICGFYPQ 600 PTEELCNRWI EVGAFYPFSR DHANYYSPRQ ELYQWDTVAD SARNALGMRY KILPFLYTLN 660 YEAHMSGAPI ARPLFFSFPE YTECYGNSRQ FLLGSSLMIS PVLEQGKTEV EALFPPGSWY 720 HMFDMTQAVV SKNGKRVTLP APLNFVNVHL YQNTILPMQQ GGLISKDART TPFSLVITFP 780 AGASEGYATG KLYLDEDELP EMKLGNGQST YVDFYASVGN GTVKMWSQVK EGKFALSKGW 840 VIEKLSVLGL KGTGQASEIQ INGSPMTKKI EVSSKEHTYV IGLEDEEENK SVMVEVRGLE 900 MLVGKDFNMS WKMGIN* 960 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam01055 | Glyco_hydro_31 | 1.0e-85 | 265 | 451 | 187 | + Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. | ||
cd06602 | GH31_MGAM_SI_GAA | 1.0e-89 | 517 | 685 | 170 | + This family includes the following three closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), and lysosomal acid alpha-glucosidase (GAA), also known as acid-maltase. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end, and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII). | ||
cd06603 | GH31_GANC_GANAB_alpha | 2.0e-96 | 284 | 667 | 390 | + This family includes the closely related glycosyl hydrolase family 31 (GH31) isozymes, neutral alpha-glucosidase C (GANC) and the alpha subunit of heterodimeric neutral alpha-glucosidase AB (GANAB). Initially distinguished on the basis of differences in electrophoretic mobility in starch gel, GANC and GANAB have been shown to have other differences, including those of substrate specificity. GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. The GANC/GANAB family includes the alpha-glucosidase II (ModA) from Dictyostelium discoideum as well as the alpha-glucosidase II (GLS2, or ROT2 - Reversal of TOR2 lethality protein 2) from Saccharomyces cerevisiae. | ||
pfam01055 | Glyco_hydro_31 | 6.0e-106 | 509 | 756 | 252 | + Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. | ||
cd06604 | GH31_glucosidase_II_MalA | 3.0e-113 | 284 | 667 | 390 | + Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a glycosyl hydrolase family 31 (GH31) enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This family also includes the MalA alpha-glucosidase from Sulfolobus sulfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source. |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAD05539.1 | 0 | 10 | 916 | 1 | 907 | alpha-xylosidase precursor [Arabidopsis thaliana] |
RefSeq | NP_177023.1 | 0 | 22 | 916 | 21 | 915 | XYL1 (ALPHA-XYLOSIDASE 1); alpha-N-arabinofuranosidase/ hydrolase, hydrolyzing O-glycosyl compounds / xylan 1,4-beta-xylosidase [Arabidopsis thaliana] |
RefSeq | XP_002311455.1 | 0 | 24 | 916 | 11 | 909 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002315944.1 | 0 | 22 | 916 | 19 | 927 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002531635.1 | 0 | 14 | 916 | 10 | 929 | alpha-glucosidase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3w38_A | 0 | 12 | 909 | 13 | 904 | A Chain A, Insight Into The Mechanism Of Enzymatic Glycosyltransfer With Retention Through The Synthesis And Analysis Of Bisubstrate Glycomimetics Of Trehalose-6-Phosphate Synthase |
PDB | 3w37_A | 0 | 12 | 909 | 13 | 904 | A Chain A, Insight Into The Mechanism Of Enzymatic Glycosyltransfer With Retention Through The Synthesis And Analysis Of Bisubstrate Glycomimetics Of Trehalose-6-Phosphate Synthase |
PDB | 3lpp_D | 0 | 61 | 911 | 105 | 898 | A Chain A, Insight Into The Mechanism Of Enzymatic Glycosyltransfer With Retention Through The Synthesis And Analysis Of Bisubstrate Glycomimetics Of Trehalose-6-Phosphate Synthase |
PDB | 3lpp_C | 0 | 61 | 911 | 105 | 898 | A Chain A, Insight Into The Mechanism Of Enzymatic Glycosyltransfer With Retention Through The Synthesis And Analysis Of Bisubstrate Glycomimetics Of Trehalose-6-Phosphate Synthase |
PDB | 3lpp_B | 0 | 61 | 911 | 105 | 898 | A Chain A, Insight Into The Mechanism Of Enzymatic Glycosyltransfer With Retention Through The Synthesis And Analysis Of Bisubstrate Glycomimetics Of Trehalose-6-Phosphate Synthase |