y
Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s11_406V6.1 |
Family | GH31 |
Protein Properties | Length: 913 Molecular Weight: 101818 Isoelectric Point: 5.1482 |
Chromosome | Chromosome/Scaffold: 11 Start: 3050784 End: 3055879 |
Description | alpha-xylosidase 1 |
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 | 276 | 764 | 0 |
FYFFAGPTPLDVVDQYTQLVGRPAPMPYWSFGFHQCKWGYKNVSELRNVVENFKKANIPLDTIWNDIDYMENYLDFTTDPVNYPEDQLRGFIEELHANGQ QYVLILDPGISTAYNNYTTLQRGLAQDIFLKDEQNKNYLAQVWPGPVFFPDFLNPKGKAWWTEEIAEFHKKVPFDGLWIDMNEVSNFCNGNRCKFSGVVY LNKNECYLVCKKPASQWDDPPYKMKRQGSYENIGDKTIALSVKHYDGTLEYNSHNLYGLSETIATNEALKSIQKKRPFILSRSTFLGSGAHTAHWTGDNA ASFKDLEYSIASMLNSGIVGLPMVGADICGFAGNTTEELCNRWIQLGAFYPFSRSHSVIDSVPQEPYVWPQVAASARSALGLRYSLLPYYYSLMFEAHNK GAPIARPLFFEFPEDPKTLHISNQFLLGSGVMVTPVIQPEVTTVNGYFPKGTWYSLFNYKSKVESNGNFFDVAAPLDSINVHIHEGTIL |
Full Sequence |
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Protein Sequence Length: 913 Download |
MKMLSMILLA AFFAVASFFV LINWDTGTMG METMSLPSGQ GHRVTSVTDL SDGRGFILDL 60 EVIEQTTLFG PDINKLRMTV RIEGQFRVHV QISDSSKPRW EIPLSLVPRN EPLAKKPNKD 120 KVELPEEPLI KLTYTTNPFG FAVTRLANDE VLFNSTPSVT TSIEGPSFTS FNTMVFKDQY 180 LEISTRLPSS AKLFGLGEST RSDGLPLVKG KTYSLWATDI GAMNANVDLY GAYPYYMDVR 240 GGGLTHGVLL LNSNGMDIEY GGDFLTWRVI GGTFDFYFFA GPTPLDVVDQ YTQLVGRPAP 300 MPYWSFGFHQ CKWGYKNVSE LRNVVENFKK ANIPLDTIWN DIDYMENYLD FTTDPVNYPE 360 DQLRGFIEEL HANGQQYVLI LDPGISTAYN NYTTLQRGLA QDIFLKDEQN KNYLAQVWPG 420 PVFFPDFLNP KGKAWWTEEI AEFHKKVPFD GLWIDMNEVS NFCNGNRCKF SGVVYLNKNE 480 CYLVCKKPAS QWDDPPYKMK RQGSYENIGD KTIALSVKHY DGTLEYNSHN LYGLSETIAT 540 NEALKSIQKK RPFILSRSTF LGSGAHTAHW TGDNAASFKD LEYSIASMLN SGIVGLPMVG 600 ADICGFAGNT TEELCNRWIQ LGAFYPFSRS HSVIDSVPQE PYVWPQVAAS ARSALGLRYS 660 LLPYYYSLMF EAHNKGAPIA RPLFFEFPED PKTLHISNQF LLGSGVMVTP VIQPEVTTVN 720 GYFPKGTWYS LFNYKSKVES NGNFFDVAAP LDSINVHIHE GTILPMQENA STTAQVMKSP 780 FTLLVAFPAA KPSGYATGKL FVDNGDDIEM VIRKGRSTFV RFIGQQSEER GVIKTKVVSG 840 DYANQERLAV EVMIILGANS APTEIKINGD LVPPSVSSTF DAAVPSLTIS GLALSVGDDF 900 ELQWFMDTRL SS* 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 | 4.0e-89 | 526 | 694 | 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). | ||
cd06602 | GH31_MGAM_SI_GAA | 5.0e-95 | 296 | 462 | 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). | ||
cd06604 | GH31_glucosidase_II_MalA | 1.0e-103 | 296 | 676 | 383 | + 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. | ||
COG1501 | COG1501 | 1.0e-128 | 178 | 869 | 706 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
pfam01055 | Glyco_hydro_31 | 0 | 277 | 764 | 493 | + 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 | XP_001753937.1 | 0 | 34 | 912 | 1 | 879 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001754376.1 | 0 | 44 | 912 | 1 | 869 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001766654.1 | 0 | 39 | 904 | 30 | 891 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001769951.1 | 0 | 37 | 904 | 28 | 891 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001779751.1 | 0 | 34 | 911 | 1 | 877 | predicted protein [Physcomitrella patens subsp. patens] |
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 | 39 | 857 | 42 | 850 | A Chain A, Crystal Structure Of Uncharacterized Conserved Protein From Thermus Thermophilus Hb8 |
PDB | 3w37_A | 0 | 39 | 857 | 42 | 850 | A Chain A, Crystal Structure Of Uncharacterized Conserved Protein From Thermus Thermophilus Hb8 |
PDB | 3l4z_A | 0 | 55 | 904 | 64 | 868 | A Chain A, Crystal Structure Of Uncharacterized Conserved Protein From Thermus Thermophilus Hb8 |
PDB | 3l4y_A | 0 | 55 | 904 | 64 | 868 | A Chain A, Crystal Structure Of Uncharacterized Conserved Protein From Thermus Thermophilus Hb8 |
PDB | 3l4x_A | 0 | 55 | 904 | 64 | 868 | A Chain A, Crystal Structure Of Uncharacterized Conserved Protein From Thermus Thermophilus Hb8 |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch degradation I | RXN-2141 | EC-3.2.1.20 | α-glucosidase |