Basic Information | |
---|---|
Species | Phaseolus vulgaris |
Cazyme ID | Phvul.003G035400.1 |
Family | GH31 |
Protein Properties | Length: 926 Molecular Weight: 102562 Isoelectric Point: 6.7904 |
Chromosome | Chromosome/Scaffold: 03 Start: 3533567 End: 3538689 |
Description | alpha-xylosidase 1 |
View CDS |
External Links |
---|
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH31 | 275 | 766 | 0 |
FYFFSGPSPLNVVDQYTTLIGRPAPMPYWAFGFHQCRWGYHNLSVVEDVVENYKKAQIPLDVIWNDDDHMDGKKDFTLNPANYPRPKLLNFLDKIHKIGM KYVVIIDPGIAVNTSYGVYQRGLANDVFIKYDGEPFLAQVWPGAVNFPDFLNPKTVSWWVDEIRRFHELVPVDGLWIDMNEVSNFCSGKCKIPKGKCPTG TGPGWICCLECKNITSTRWDDPPYKINASGIKAPIGYKTIATSAYHYNGVLEYDAHSLYGFAQSAATHKGLQGLQGKRPFILSRSTYVGSGKYAAHWTGD NQGTWENLKYSISTMLNFGIFGVPMVGSDICGFYPQPTEELCNRWIEVGAFYPFSRDHANYYSPRQELYQWQSVAESARNALGIRYKLLPFLYTLNYEAH VSGAPIARPLFFSFPTYTECYGLSTQFLLGTSLMVSPVLEQGKTQVKALFAPGSWYSLLDWTQTITSKDGVYVTLDAPLHVVNVHLYQNTIL |
Full Sequence |
---|
Protein Sequence Length: 926 Download |
MVSSNHLAAI SLSSLLLVLL LCSAGASSSS KNATKIGQGY RLVSIEETPD GGLVGILQVK 60 EKTKTYGSDI PLLRFYVKHE TDNRLRVHIT DAQKQRWEVP YNLLPREQPP PLTQSIGKFR 120 KNPITVSEYS GSEFLFSYTS DPFSFVVKRK SNGETLFDTS SSDSDPFSSL VFKDQYLEIS 180 TKLPKSASLY GLGENTQPHG IKLYPSDPYT LYTTDISAIN LNADLYGSHP VYMDLRNAGG 240 KASAHGVLLL NSNGMDVFYT GTSLTYKIIG GVFDFYFFSG PSPLNVVDQY TTLIGRPAPM 300 PYWAFGFHQC RWGYHNLSVV EDVVENYKKA QIPLDVIWND DDHMDGKKDF TLNPANYPRP 360 KLLNFLDKIH KIGMKYVVII DPGIAVNTSY GVYQRGLAND VFIKYDGEPF LAQVWPGAVN 420 FPDFLNPKTV SWWVDEIRRF HELVPVDGLW IDMNEVSNFC SGKCKIPKGK CPTGTGPGWI 480 CCLECKNITS TRWDDPPYKI NASGIKAPIG YKTIATSAYH YNGVLEYDAH SLYGFAQSAA 540 THKGLQGLQG KRPFILSRST YVGSGKYAAH WTGDNQGTWE NLKYSISTML NFGIFGVPMV 600 GSDICGFYPQ PTEELCNRWI EVGAFYPFSR DHANYYSPRQ ELYQWQSVAE SARNALGIRY 660 KLLPFLYTLN YEAHVSGAPI ARPLFFSFPT YTECYGLSTQ FLLGTSLMVS PVLEQGKTQV 720 KALFAPGSWY SLLDWTQTIT SKDGVYVTLD APLHVVNVHL YQNTILPMQQ GGLVSKEARM 780 TPFTLIVTFP SGAAEGEAKG NLFLDNDELP DMNLGNGYST YVDLYATVKQ GAVKVWSDVQ 840 EGKFALDKGL IIDAISVLGL DGTGAVSSFE IDGKPLTGVP SVNISTSQHE HLNSEGEGEK 900 KTVMVALKGL NIPVGKNFAM TWKMG* |
Functional Domains Download unfiltered results here | ||||||
---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
PLN02763 | PLN02763 | 3.0e-84 | 182 | 729 | 561 | + hydrolase, hydrolyzing O-glycosyl compounds |
cd06602 | GH31_MGAM_SI_GAA | 2.0e-89 | 295 | 459 | 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 | 2.0e-91 | 527 | 695 | 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). |
cd06604 | GH31_glucosidase_II_MalA | 3.0e-120 | 295 | 677 | 389 | + 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 | 276 | 766 | 497 | + 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 | |
---|---|
GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CAA10382.2 | 0 | 27 | 925 | 32 | 934 | alpha-D-xylosidase [Tropaeolum majus] |
RefSeq | XP_002282429.1 | 0 | 15 | 925 | 7 | 921 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002311455.1 | 0 | 28 | 925 | 7 | 907 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002315944.1 | 0 | 28 | 925 | 24 | 925 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002531635.1 | 0 | 8 | 925 | 4 | 927 | alpha-glucosidase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3w38_A | 0 | 15 | 891 | 18 | 883 | A Chain A, Structure Of Beta2-Bungarotoxin: Potassium Channel Binding By Kunitz Modules And Targeted Phospholipase Act |
PDB | 3w37_A | 0 | 15 | 891 | 18 | 883 | A Chain A, Structure Of Beta2-Bungarotoxin: Potassium Channel Binding By Kunitz Modules And Targeted Phospholipase Act |
PDB | 3lpp_D | 0 | 38 | 922 | 79 | 898 | A Chain A, Structure Of Beta2-Bungarotoxin: Potassium Channel Binding By Kunitz Modules And Targeted Phospholipase Act |
PDB | 3lpp_C | 0 | 38 | 922 | 79 | 898 | A Chain A, Structure Of Beta2-Bungarotoxin: Potassium Channel Binding By Kunitz Modules And Targeted Phospholipase Act |
PDB | 3lpp_B | 0 | 38 | 922 | 79 | 898 | A Chain A, Structure Of Beta2-Bungarotoxin: Potassium Channel Binding By Kunitz Modules And Targeted Phospholipase Act |