y
Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10041457 |
Family | GH31 |
Protein Properties | Length: 937 Molecular Weight: 104129 Isoelectric Point: 6.7084 |
Chromosome | Chromosome/Scaffold: 272 Start: 171113 End: 176215 |
Description | alpha-xylosidase 1 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH31 | 276 | 767 | 0 |
FYFFSGPSPLGVIDQYTSLVGRPAPMPYWSFGFHQCRWGYHNLSVVEDVVENYKKAKIPLDVIWNDDDHMDFHKDFTLSPVSYPREKLAAFLEKVHGMGM KYIVLIDPGINVNSTYGVYQRGIADDVFIKYEGQNFLAQVWPGAVYFPDFLNPKTVSWWGDEIRRFHEMVPVDGLWIDMNEASNFCTGLCTIPKGKKCPT GTGPGWNCCLDCKNITKTRWDEPPYKINASGIQSPIGYKTIATSATHYNGVLEYDAHSLYGFSQAIATHKALQNLQGKRPFILSRSTYVGSGKYTAHWTG DNQGTWENLKYSISTMLNFGIFGVPMVGADICGFYPQPTEELCNRWIEVGAFYPFSRDHANFYSPRQELYQWESVAESARNALGLRYKLLPYLYTLSYEA HNTGAPITRPLFFSFPTYTDCYGLSTQFLLGSSLMISPVLEQGKSQVKALFPPGSWYSMFDMSKAINSKGEYYTLDAPLHVVNVHLYQNTIL |
Full Sequence |
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Protein Sequence Length: 937 Download |
MVLSPSSSLL LPFLLLLLCF HGVTSKKSSS SSVPSKIGKG YRLISIEKAP DGGFLGHLQV 60 KQKNSVYGSD IPLLQLYVKH ETDDRLRVHI TDAEKQRWEV PYNLLPRENP PVAKQTIGKS 120 RKNLIGVQDY TNSGELIFSY TADPFSFAVR RKSDGETLFN TSSDGSSFGP MVFKDQYLEI 180 STKLPPDASL YGLGENTQAN GIKLKPGEPY TLYTLDISAI NLNTDLYGSH PVYMDLRNVQ 240 GKPNAHGVLL LNSNGMDVFY RGNSLTYKVI GGVFDFYFFS GPSPLGVIDQ YTSLVGRPAP 300 MPYWSFGFHQ CRWGYHNLSV VEDVVENYKK AKIPLDVIWN DDDHMDFHKD FTLSPVSYPR 360 EKLAAFLEKV HGMGMKYIVL IDPGINVNST YGVYQRGIAD DVFIKYEGQN FLAQVWPGAV 420 YFPDFLNPKT VSWWGDEIRR FHEMVPVDGL WIDMNEASNF CTGLCTIPKG KKCPTGTGPG 480 WNCCLDCKNI TKTRWDEPPY KINASGIQSP IGYKTIATSA THYNGVLEYD AHSLYGFSQA 540 IATHKALQNL QGKRPFILSR STYVGSGKYT AHWTGDNQGT WENLKYSIST MLNFGIFGVP 600 MVGADICGFY PQPTEELCNR WIEVGAFYPF SRDHANFYSP RQELYQWESV AESARNALGL 660 RYKLLPYLYT LSYEAHNTGA PITRPLFFSF PTYTDCYGLS TQFLLGSSLM ISPVLEQGKS 720 QVKALFPPGS WYSMFDMSKA INSKGEYYTL DAPLHVVNVH LYQNTILPMQ RGGMISRDAR 780 TTPFTLVVTF PAGASDGEEA KGSLFIDNDE LPEMKLGNGE SSYVDFYATV SKGVVKMWSE 840 VQEGKFALSK GLTIEKVSVL GLGGSGSSPS EVEVDGKAMS SKVQVSTMEQ MYMESPSSSL 900 NGGDGDEKAK KSMMVEVSGL EIPVGKNFAM TWHMGV* 960 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06602 | GH31_MGAM_SI_GAA | 2.0e-85 | 296 | 460 | 169 | + 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). | ||
cd06602 | GH31_MGAM_SI_GAA | 4.0e-93 | 529 | 692 | 165 | + 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). | ||
COG1501 | COG1501 | 2.0e-117 | 47 | 856 | 843 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
cd06604 | GH31_glucosidase_II_MalA | 7.0e-118 | 296 | 679 | 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. | ||
pfam01055 | Glyco_hydro_31 | 0 | 277 | 767 | 496 | + Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. |
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 |
RefSeq | NP_177023.1 | 0 | 19 | 936 | 21 | 914 | XYL1 (ALPHA-XYLOSIDASE 1); alpha-N-arabinofuranosidase/ hydrolase, hydrolyzing O-glycosyl compounds / xylan 1,4-beta-xylosidase [Arabidopsis thaliana] |
RefSeq | XP_002282429.1 | 0 | 6 | 936 | 3 | 922 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002311455.1 | 0 | 25 | 936 | 3 | 908 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002315944.1 | 0 | 19 | 936 | 19 | 926 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002531635.1 | 0 | 5 | 936 | 3 | 928 | 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 | 8 | 862 | 15 | 851 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3w37_A | 0 | 8 | 862 | 15 | 851 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3lpp_D | 0 | 65 | 932 | 104 | 898 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3lpp_C | 0 | 65 | 932 | 104 | 898 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3lpp_B | 0 | 65 | 932 | 104 | 898 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |