| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G428518_T03 |
| Family | GH31 |
| Protein Properties | Length: 675 Molecular Weight: 75076.2 Isoelectric Point: 7.3707 |
| Chromosome | Chromosome/Scaffold: 6 Start: 91630823 End: 91633817 |
| Description | Glycosyl hydrolases family 31 protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH31 | 266 | 599 | 0 |
| YFFAGPSPLDVVDQYTQLIGRPAPMPYWSFGFHQCRYGYKNLADLEGVVAGYAKARIPLEVMWTDIDYMDAFKDFTLDPVNFPAGPMRQFVDRLHRNGQK YVVIIDPGISVNETYGTYVRGMQQDVFLKRNGTNYLGKVWPGYVYFPDFLNPRAAEFWAREIALFRRTLPVDGLWIDMNEVSNFVDPAPLNALDDPPYRI NNSGVHRPINNKTTPASAVHYGGVRDYDAHNLYGFLEARATHGALLADTGRRPFVLSRSTFVGSGRYTAHWTGDNAATWDDLRYSINTMLSFGLFGIPMV GADICGFGGNTTEELCSRWIQVQAFHALQDQHAM | |||
| Full Sequence |
|---|
| Protein Sequence Length: 675 Download |
| MALSWSPAVV VFLLLLLLLP APWPRAAAQA GRYHAVSVSR AGGQLSARLE LAGAGAGGQK 60 PELGPDVQRL SLTASLETDS RLHVRITDAD HRRWEVPQSV IPREAPRDDV PLEASTGASP 120 PHSRVLSAAT SDLAFTLHAS PFRFTVSRRS SGDALFDTSA ALVFKDRYLE LTTALPPEGG 180 ASLYGLGEHT KRTFRLQRND TFTMWNADIP AANADVNLYG SHPFYLDVRH AGAAHGVLLL 240 NSNGMDVEYG GSYLTYKVIG GVLDLYFFAG PSPLDVVDQY TQLIGRPAPM PYWSFGFHQC 300 RYGYKNLADL EGVVAGYAKA RIPLEVMWTD IDYMDAFKDF TLDPVNFPAG PMRQFVDRLH 360 RNGQKYVVII DPGISVNETY GTYVRGMQQD VFLKRNGTNY LGKVWPGYVY FPDFLNPRAA 420 EFWAREIALF RRTLPVDGLW IDMNEVSNFV DPAPLNALDD PPYRINNSGV HRPINNKTTP 480 ASAVHYGGVR DYDAHNLYGF LEARATHGAL LADTGRRPFV LSRSTFVGSG RYTAHWTGDN 540 AATWDDLRYS INTMLSFGLF GIPMVGADIC GFGGNTTEEL CSRWIQVQAF HALQDQHAMS 600 TDMYELSFRC LLVKLGAFYP FARDHSAIGT VRRELYLWEL VARSARKALG LRYRLLPYMY 660 TLMYEAHTTG APIAR 720 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG1501 | COG1501 | 1.0e-108 | 130 | 675 | 557 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
| cd06600 | GH31_MGAM-like | 2.0e-111 | 285 | 670 | 389 | + 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 | 3.0e-126 | 285 | 670 | 392 | + 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 | 2.0e-175 | 266 | 675 | 413 | + 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 | 0 | 285 | 675 | 396 | + 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). | ||
| 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 | EAZ02070.1 | 0 | 66 | 675 | 70 | 648 | hypothetical protein OsI_24149 [Oryza sativa Indica Group] |
| GenBank | EEC81171.1 | 0 | 65 | 675 | 66 | 660 | hypothetical protein OsI_24144 [Oryza sativa Indica Group] |
| RefSeq | NP_001058347.1 | 0 | 65 | 675 | 66 | 648 | Os06g0675700 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001058353.1 | 0 | 66 | 675 | 70 | 648 | Os06g0676700 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | XP_002438844.1 | 0 | 29 | 675 | 39 | 663 | hypothetical protein SORBIDRAFT_10g027110 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3w38_A | 0 | 39 | 675 | 54 | 676 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
| PDB | 3w37_A | 0 | 39 | 675 | 54 | 676 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
| PDB | 3ctt_A | 0 | 61 | 675 | 76 | 653 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
| PDB | 2qmj_A | 0 | 61 | 675 | 76 | 653 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
| PDB | 2qly_A | 0 | 61 | 675 | 76 | 653 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
