y
Basic Information | |
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Species | Chlamydomonas reinhardtii |
Cazyme ID | Cre03.g194700.t1.3 |
Family | GH31 |
Protein Properties | Length: 1287 Molecular Weight: 134969 Isoelectric Point: 6.1492 |
Chromosome | Chromosome/Scaffold: 3 Start: 6447765 End: 6456076 |
Description | alpha-xylosidase 1 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH31 | 367 | 929 | 0 |
WLLAGPTPEDVSRQYLQLVGAPALPPRWALGFHQSRYGYADVSELEAVVAGFEAAQLPLEVLWSDIDMYDRARMFTTDSERYPVDRLRGLVDRLHGSGRR WVPIVDCGITALPGQAYPPYDRGLAAGVFLRDSGGRQPLLGQVWSGPTHWPDFLHPNTSEYWGGLLSDMAARLPYDGLWLDMNEPSNFCTGQCRLRQSPG HVQGGGGAEAVNGRNDGNANSRQWGKRDVADEAGIWEGARRPETVGMRREVGAGAKAVTTRPAARLRLQQLGISCDLDCTAPSPDDPLSYPPYAVNNGNR RAPLYVNTVPMNAVGYGGVRQYDSHNLYALAEVAVTHGALQAILPGSRPFILTRSTWAGSGRYAAHWSGDNGASWEDLARGGGSLLAASLAGISMAGADV CGFWGATSEQLCARWLAAGSFYTFTRDHSDHSPQEPYRFPAAAQAARNSLRARYALLPYLYTALYDVHTGRAGTVARPLAWEFPSDPRVADLSTQWLLGD SLLVAPVLRPDTDWTEAVFPAGARSTWCRLSDLGDCHTGPAQHLVQSPLGSEPPLFLRAGAII |
Full Sequence |
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Protein Sequence Length: 1287 Download |
MLVLLLYGIS RFSIAAGIGP NTQGCSPEGP RSDCGYYGIQ QAECEQRGCC WFPVAAAAAA 60 TAADGRGTES SASGRAAPAT DTIGSHNDIP WCFHPNAVQT VYAVQSVEKV DPGGSGAVTR 120 MLLQLRPGPA AVPELGPDFE MLQVELQQQT PQRLYLRVSP LPSPGGGGAG GAATGQAQSQ 180 PHQERWRVPE QLLPRPPPPT ALPEAPLYQL QLPQPGDDFS LHVTRQPESQ AEVAAEAGTE 240 AAVEAAAAGQ SLLEVLGGSC LVFKPQYLQL RMRVPQQTNL YGMGEATLPD GLRLRRDGVA 300 RALWNSDTPA AAVGVNLYGS HPVLYGIVPG SGGTAWGVFL ANSNAMEFAA GSNDVTFRLT 360 GGDLELWLLA GPTPEDVSRQ YLQLVGAPAL PPRWALGFHQ SRYGYADVSE LEAVVAGFEA 420 AQLPLEVLWS DIDMYDRARM FTTDSERYPV DRLRGLVDRL HGSGRRWVPI VDCGITALPG 480 QAYPPYDRGL AAGVFLRDSG GRQPLLGQVW SGPTHWPDFL HPNTSEYWGG LLSDMAARLP 540 YDGLWLDMNE PSNFCTGQCR LRQSPGHVQG GGGAEAVNGR NDGNANSRQW GKRDVADEAG 600 IWEGARRPET VGMRREVGAG AKAVTTRPAA RLRLQQLGIS CDLDCTAPSP DDPLSYPPYA 660 VNNGNRRAPL YVNTVPMNAV GYGGVRQYDS HNLYALAEVA VTHGALQAIL PGSRPFILTR 720 STWAGSGRYA AHWSGDNGAS WEDLARGGGS LLAASLAGIS MAGADVCGFW GATSEQLCAR 780 WLAAGSFYTF TRDHSDHSPQ EPYRFPAAAQ AARNSLRARY ALLPYLYTAL YDVHTGRAGT 840 VARPLAWEFP SDPRVADLST QWLLGDSLLV APVLRPDTDW TEAVFPAGAR STWCRLSDLG 900 DCHTGPAQHL VQSPLGSEPP LFLRAGAIIP TQPFRPAATT TAEVAASPLA LTALLSSASE 960 ASGSSSNSSS SGSAEGGGGP PAPLVEEDVD WVAAGRLYAD NGTDPRVDGA DCLRVELRAG 1020 ALLAAGTGYL AYEVQRPPAV AVEAGSSSGR GSQGRGSSSG SSSKLPQDGT GSSSGNDSSS 1080 GGGGGGVAAG GGVRTAGGGA DTDVRLLRVA EVVVVGVVLP PGAGAFEVQV EVGGQLKPPE 1140 QPRGAKRSVK RPGGHSLQSQ SQVPRRLAGW AAAGGSSANS RNGGEVVGMW DGDGAGGGCG 1200 HASHQEVMRR RKPAQAQASA RGARVPVPAT AVEFDPVRQL LRVRGLELSA VVSFRLEWKP 1260 LTAPPHSTTG FSSVPRWQPE EARAAA* 1320 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06604 | GH31_glucosidase_II_MalA | 2.0e-51 | 386 | 554 | 169 | + 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. | ||
cd06602 | GH31_MGAM_SI_GAA | 6.0e-53 | 688 | 854 | 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). | ||
pfam01055 | Glyco_hydro_31 | 2.0e-56 | 680 | 929 | 256 | + Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. | ||
pfam01055 | Glyco_hydro_31 | 3.0e-64 | 367 | 557 | 191 | + 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-81 | 386 | 554 | 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). |
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 | EEQ42202.1 | 0 | 52 | 1048 | 7 | 903 | glucoamylase 1 precursor [Candida albicans WO-1] |
Swiss-Prot | O74254 | 0 | 53 | 1048 | 22 | 903 | AMYG_CANAL RecName: Full=Glucoamylase 1; AltName: Full=Glucan 1,4-alpha-glucosidase; AltName: Full=1,4-alpha-D-glucan glucohydrolase; Flags: Precursor |
RefSeq | XP_001693117.1 | 0 | 141 | 559 | 1 | 419 | alpha glucosidase [Chlamydomonas reinhardtii] |
RefSeq | XP_001693117.1 | 0 | 649 | 1286 | 422 | 1059 | alpha glucosidase [Chlamydomonas reinhardtii] |
RefSeq | XP_723581.1 | 0 | 53 | 1048 | 22 | 903 | hypothetical protein CaO19.4899 [Candida albicans SC5314] |
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 | 102 | 580 | 45 | 506 | A Chain A, Structural Determinants For Ca2+ And Pip2 Binding By The C2a Domain Of Rabphilin |
PDB | 3w38_A | 0 | 640 | 963 | 473 | 791 | A Chain A, Structural Determinants For Ca2+ And Pip2 Binding By The C2a Domain Of Rabphilin |
PDB | 3w37_A | 0 | 102 | 580 | 45 | 506 | A Chain A, Structural Determinants For Ca2+ And Pip2 Binding By The C2a Domain Of Rabphilin |
PDB | 3w37_A | 0 | 640 | 963 | 473 | 791 | A Chain A, Structural Determinants For Ca2+ And Pip2 Binding By The C2a Domain Of Rabphilin |
PDB | 3ctt_A | 0 | 24 | 557 | 14 | 453 | A Chain A, Structural Determinants For Ca2+ And Pip2 Binding By The C2a Domain Of Rabphilin |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch degradation I | RXN-2141 | EC-3.2.1.20 | α-glucosidase |