y
Basic Information | |
---|---|
Species | Brachypodium distachyon |
Cazyme ID | Bradi1g32650.1 |
Family | GH31 |
Protein Properties | Length: 897 Molecular Weight: 97765.5 Isoelectric Point: 7.5441 |
Chromosome | Chromosome/Scaffold: 1 Start: 28071535 End: 28075392 |
Description | Glycosyl hydrolases family 31 protein |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH31 | 264 | 754 | 0 |
FYFFAGPTPLAVVDQYTDLVGRPAPMPYWSFGFHQCRYGYENVNDLERVVAGYAEAKIPLEVMWTDIDYMDSFKDFTLNRVNFSAAELRPFVDRLHRNAQ KYVLILDPGTTTSRSIQLIAPTTFSLIDLVAGISIIDPKYGTFIRGMEAGIFLKRNGTEFRGNVWPGDVYFPDFLNPRAAEFWAREISLFRRTIPVDGLW IDMNEISNFFNPDPLTPLDEPPYSINNQGDRRTINYKTAAASATHYGGVSEFDAHNLFGLLESRATHAALLRDTGRRPFVLSRSTFVGSGRYTAHWTGDN DATWGDLRYSINTMLSFGLFGMPMVGADICGFGKNTTEELCGRWIQLGAFYPFSRDHSAIFTVRRELYLWDSVARSARKALGLRYRLLPYLYTLMYQAHV SGAPMARPLFFSFPDDAATYGVDAQFMLGRAVLVSPVLQPGATSVEAYFPAGRWFSLFDHSSVVVSKVGKRVTLPAPADTVNVHVAGGSIV |
Full Sequence |
---|
Protein Sequence Length: 897 Download |
MAMAGSPSAA GSCHLPALLL FLAAVPWGVD CAGAGAGTYD VVSVTSSGSQ LSAGLELAAA 60 GGVDPALGPD VQRLHLTASL ETNTRLQVRI TDADRPRWEI PQDILPRPTP EHVVPYKPLA 120 SPGSRVLSAP GSDLVFTLHS SPFRFTVARV SNGDVLFDSL PRLVFKDQYL ELTTALPSER 180 ANLYGLGEQT KQSFRLRHGD TFTLWNADIA AATVDVNLYG SHPFYMDLRA GAAHGVLLLN 240 SNGMDVVYGG SSLTYKVIGG ILDFYFFAGP TPLAVVDQYT DLVGRPAPMP YWSFGFHQCR 300 YGYENVNDLE RVVAGYAEAK IPLEVMWTDI DYMDSFKDFT LNRVNFSAAE LRPFVDRLHR 360 NAQKYVLILD PGTTTSRSIQ LIAPTTFSLI DLVAGISIID PKYGTFIRGM EAGIFLKRNG 420 TEFRGNVWPG DVYFPDFLNP RAAEFWAREI SLFRRTIPVD GLWIDMNEIS NFFNPDPLTP 480 LDEPPYSINN QGDRRTINYK TAAASATHYG GVSEFDAHNL FGLLESRATH AALLRDTGRR 540 PFVLSRSTFV GSGRYTAHWT GDNDATWGDL RYSINTMLSF GLFGMPMVGA DICGFGKNTT 600 EELCGRWIQL GAFYPFSRDH SAIFTVRREL YLWDSVARSA RKALGLRYRL LPYLYTLMYQ 660 AHVSGAPMAR PLFFSFPDDA ATYGVDAQFM LGRAVLVSPV LQPGATSVEA YFPAGRWFSL 720 FDHSSVVVSK VGKRVTLPAP ADTVNVHVAG GSIVPMQGHA LTTARARRTA FRLLVALAED 780 GTAAGELFVD DGESPEMGGT RSKFSLVRFT SSTGTDGVVR VRSQVVHDSY KPSRRMVIGK 840 VVVMGIKRPA PMKKLSVRVN GAEVKAASME AGTGLGVAHV GGLSLVVGQP FELAIS* 900 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06600 | GH31_MGAM-like | 3.0e-92 | 284 | 635 | 354 | + This family includes the following closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), lysosomal acid alpha-glucosidase (GAA), neutral alpha-glucosidase C (GANC), the alpha subunit of neutral alpha-glucosidase AB (GANAB), and alpha-glucosidase II. 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). 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. Alpha-glucosidase II is a 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. The MGAM-like family corresponds to subgroup 1 in the Ernst et al classification of GH31 enzymes. | ||
cd06604 | GH31_glucosidase_II_MalA | 2.0e-101 | 284 | 631 | 350 | + 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 | 2.0e-125 | 94 | 849 | 771 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
cd06602 | GH31_MGAM_SI_GAA | 1.0e-174 | 284 | 683 | 404 | + 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 | 0 | 265 | 754 | 494 | + 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 |
GenBank | AAF76254.1 | 0 | 70 | 896 | 64 | 876 | high pI alpha-glucosidase [Hordeum vulgare subsp. vulgare] |
GenBank | ACZ37244.1 | 0 | 70 | 896 | 64 | 876 | alpha-glucosidase [Hordeum vulgare subsp. vulgare] |
GenBank | ACZ37245.1 | 0 | 70 | 896 | 66 | 878 | alpha-glucosidase [Hordeum vulgare subsp. spontaneum] |
GenBank | ACZ37246.1 | 0 | 70 | 896 | 65 | 877 | alpha-glucosidase [Hordeum vulgare subsp. spontaneum] |
GenBank | ACZ37249.1 | 0 | 70 | 896 | 64 | 876 | alpha-glucosidase [Hordeum vulgare subsp. vulgare] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3w38_A | 0 | 30 | 896 | 39 | 907 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3w37_A | 0 | 30 | 896 | 39 | 907 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ctt_A | 0 | 24 | 891 | 40 | 864 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 2qmj_A | 0 | 24 | 891 | 40 | 864 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 2qly_A | 0 | 24 | 891 | 40 | 864 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
Metabolic Pathways | |||
---|---|---|---|
Pathway Name | Reaction | EC | Protein Name |
starch degradation I | RXN-2141 | EC-3.2.1.20 | α-glucosidase |