y
Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.007G026900.1 |
Family | GH31 |
Protein Properties | Length: 927 Molecular Weight: 104259 Isoelectric Point: 6.3761 |
Chromosome | Chromosome/Scaffold: 07 Start: 1972079 End: 1976296 |
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 | 275 | 767 | 0 |
FYFFAGPTPLNVVDQYTSLIGRPAPMPYWAFGFHQCRWGYHNLSVVEDVVDNYKKAKIPLDVIWNDDDHMDGHKDFTLNPTNYPHSKLLDFLDKIHSIGM KYIVIIDPGIAVNSSYGVYQRGMANDVFIKYEGEPFLAQVWPGAVNFPDFLNPKTVSWWVDEIRRFHELVPIDGLWIDMNEASNFCSGKCRIPEGKVCPS GTGPGWICCLDCKNITSTRWDEPPYKINASGVQAPIGFKTIATSAVHYNGVLEYDAHSIYGFSQSIATHKALQGLQGKRPFILSRSTYVGSGKYVAHWTG DNKGTWEDLRYSISTMLNFGIFGVPMVGSDICGFYPAPTEELCNRWIEVGAFYPFSRDHANFYSPRQELYQWESVAESARNALGMRYKLLPYLYTLNYEA HNSGAPIARPLFFSFPSYTECYDLNTQFLLGSSLMVSPVVEQGKTQVKALFPPGTWYSLFDLTQTIVSKDGNYVTLDAPLHVVNVHLYQNTIL |
Full Sequence |
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Protein Sequence Length: 927 Download |
MLSSHTLPPL LSLSFLLLTC FLYVVAEEPN LSNKIGQGYR LISIKNAPDG TLVGLLQVKQ 60 KNNIYGPDIP LLRLHVKQET ENRLRVHITD AEKQRWEVPY NLLPREQPLS VKQNTEWSWS 120 WSRKKNNLIS LSNSSELVFS YTSDPFSFAV KRKSNGDTLF DSSSNEFNTL VFKDQYLEIS 180 TKLPKDVSLY GLGENTQPHG MKLYPSDPYT LYTTNVSAIN LNTDLYSAHP VYMDLRNEGD 240 EPYAHGVLLL NSNAMDVFYR GTSLTYKVIG GVFDFYFFAG PTPLNVVDQY TSLIGRPAPM 300 PYWAFGFHQC RWGYHNLSVV EDVVDNYKKA KIPLDVIWND DDHMDGHKDF TLNPTNYPHS 360 KLLDFLDKIH SIGMKYIVII DPGIAVNSSY GVYQRGMAND VFIKYEGEPF LAQVWPGAVN 420 FPDFLNPKTV SWWVDEIRRF HELVPIDGLW IDMNEASNFC SGKCRIPEGK VCPSGTGPGW 480 ICCLDCKNIT STRWDEPPYK INASGVQAPI GFKTIATSAV HYNGVLEYDA HSIYGFSQSI 540 ATHKALQGLQ GKRPFILSRS TYVGSGKYVA HWTGDNKGTW EDLRYSISTM LNFGIFGVPM 600 VGSDICGFYP APTEELCNRW IEVGAFYPFS RDHANFYSPR QELYQWESVA ESARNALGMR 660 YKLLPYLYTL NYEAHNSGAP IARPLFFSFP SYTECYDLNT QFLLGSSLMV SPVVEQGKTQ 720 VKALFPPGTW YSLFDLTQTI VSKDGNYVTL DAPLHVVNVH LYQNTILPMQ QGGMVSKDAR 780 MTPFSLIVTF PAGATDGVAK GKLFLDDDEL PEMKLGSGFS TYIDFHATVK EGNVKVWSEV 840 QEGKFALDKG WVIDTIKVLG LSRNGTLTEI EIDGEKQMNI LSVEVSTSQH NYLFGHGDGD 900 KILMVGLKRL NIPLGKNFAV TWKMGS* 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 | 8.0e-87 | 276 | 463 | 188 | + 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-92 | 528 | 696 | 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 | 6.0e-99 | 295 | 678 | 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 | 3.0e-110 | 520 | 767 | 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 | 1.0e-118 | 295 | 678 | 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 |
EMBL | CAA10382.2 | 0 | 29 | 925 | 35 | 934 | alpha-D-xylosidase [Tropaeolum majus] |
RefSeq | XP_002282429.1 | 0 | 11 | 925 | 1 | 921 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002311455.1 | 0 | 33 | 925 | 13 | 907 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002315944.1 | 0 | 10 | 925 | 4 | 925 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002531635.1 | 0 | 1 | 925 | 1 | 927 | 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 | 11 | 891 | 14 | 882 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
PDB | 3w37_A | 0 | 11 | 891 | 14 | 882 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
PDB | 3lpp_D | 0 | 64 | 922 | 105 | 898 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
PDB | 3lpp_C | 0 | 64 | 922 | 105 | 898 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
PDB | 3lpp_B | 0 | 64 | 922 | 105 | 898 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |