y
Basic Information | |
---|---|
Species | Glycine max |
Cazyme ID | Glyma15g14150.1 |
Family | GH31 |
Protein Properties | Length: 938 Molecular Weight: 104949 Isoelectric Point: 7.1502 |
Chromosome | Chromosome/Scaffold: 15 Start: 10667127 End: 10671818 |
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 | 315 | 783 | 0 |
FYFFVGSTPELVLEQYTEFIGRPAPMPYWSFGFHQCRYGYKNVSDLQDVVANYAKASIPLEVMWTDIDYMDAYKDFTFDPINFPLDKMRSFVDTLHKNGQ KYVLIVDPGISVNETYATYIRGLQADVYIKRNGSNYLGKVWPGPVYYPDFLNPRSQAFWGREIKLFRDLLPIDGLWIDMNELSNFITSPPIPFSNLDNPP YKINNVGDQHSINDRTVPATSLHFGNITEYNVHNLYGLLESKVTNKALKDITGKRPFILSRSTFVSSGKYAAHWTGDNAATWNDLAYSIPAILNSGIFGI PMVGADICGFGGNTTEELCRRWIQLGAFYPFARDHSDKNSNRQELYLWDSVADSAKKVLGLRYRLLPYLYTLMYEAHTKGTPIARPLFFSFPEDVTTYEI SSQFLLGKGVLVSPVLQSGATSVVAYFPKGSWFDLFNVSNSVNAESGKYVTLDAPSDHINVHVGEGNIL |
Full Sequence |
---|
Protein Sequence Length: 938 Download |
MRNNSEVNLP RLHHAIISYP YSHTHFNTNT MATRWRVTKA TATIFSVFLI FCSSFSSLEA 60 TPVGYGYTIS TVYNFPITNS LTANLDLIKP SSVFGPDIPH LSLTASFENK DRLRVRITDS 120 NHQRWEIPQE VIPRGSSFQY YPLRSLNSKQ GSPQKKHSFS LTHPNSDLVF TLHNTTPFGF 180 TVSRKSSNDV LFNTAPNPSN PETFLIFKDQ YLQLSSSLPS QRASLFGLGE HTKSSFKLRP 240 NQTLTLWTAD IASANLDLNL YGSHPFYLDV RSSSFDGKVK AGTTHGVLLF NSNGMDIMYG 300 GDQITYKVIG GVFDFYFFVG STPELVLEQY TEFIGRPAPM PYWSFGFHQC RYGYKNVSDL 360 QDVVANYAKA SIPLEVMWTD IDYMDAYKDF TFDPINFPLD KMRSFVDTLH KNGQKYVLIV 420 DPGISVNETY ATYIRGLQAD VYIKRNGSNY LGKVWPGPVY YPDFLNPRSQ AFWGREIKLF 480 RDLLPIDGLW IDMNELSNFI TSPPIPFSNL DNPPYKINNV GDQHSINDRT VPATSLHFGN 540 ITEYNVHNLY GLLESKVTNK ALKDITGKRP FILSRSTFVS SGKYAAHWTG DNAATWNDLA 600 YSIPAILNSG IFGIPMVGAD ICGFGGNTTE ELCRRWIQLG AFYPFARDHS DKNSNRQELY 660 LWDSVADSAK KVLGLRYRLL PYLYTLMYEA HTKGTPIARP LFFSFPEDVT TYEISSQFLL 720 GKGVLVSPVL QSGATSVVAY FPKGSWFDLF NVSNSVNAES GKYVTLDAPS DHINVHVGEG 780 NILALQGEAI TTVAARKTAF QLVVVISNSG SSFGQVYLDD GEALDIAGVN DQWTLASFYG 840 ALHNNSVLVT SKVTNARFAL DQRWIIDNVS FLGIPKNKRF NGMDLAGNEL KIVNGMDSMR 900 TAVVKSEFDS SSQFVNVQVS KLSLPIGEEF KLEIEIK* 960 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06600 | GH31_MGAM-like | 3.0e-98 | 335 | 694 | 363 | + 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 | 8.0e-114 | 335 | 694 | 366 | + 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 | 4.0e-118 | 226 | 822 | 608 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
pfam01055 | Glyco_hydro_31 | 0 | 316 | 783 | 472 | + 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 | 335 | 712 | 383 | + 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 |
EMBL | CAN66951.1 | 0 | 45 | 936 | 10 | 898 | hypothetical protein [Vitis vinifera] |
EMBL | CBI39013.1 | 0 | 4 | 936 | 866 | 1759 | unnamed protein product [Vitis vinifera] |
EMBL | CBI39013.1 | 0 | 49 | 923 | 19 | 859 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002317678.1 | 0 | 63 | 936 | 47 | 912 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317679.1 | 0 | 44 | 935 | 23 | 903 | predicted protein [Populus trichocarpa] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3w38_A | 0 | 59 | 937 | 37 | 909 | A Chain A, Solution Structure Of The C-Terminal Domain Ole E 9 |
PDB | 3w37_A | 0 | 59 | 937 | 37 | 909 | A Chain A, Solution Structure Of The C-Terminal Domain Ole E 9 |
PDB | 3l4z_A | 0 | 81 | 838 | 65 | 789 | A Chain A, Solution Structure Of The C-Terminal Domain Ole E 9 |
PDB | 3l4y_A | 0 | 81 | 838 | 65 | 789 | A Chain A, Solution Structure Of The C-Terminal Domain Ole E 9 |
PDB | 3l4x_A | 0 | 81 | 838 | 65 | 789 | A Chain A, Solution Structure Of The C-Terminal Domain Ole E 9 |
Metabolic Pathways | |||
---|---|---|---|
Pathway Name | Reaction | EC | Protein Name |
starch degradation I | RXN-2141 | EC-3.2.1.20 | α-glucosidase |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
HO795307 | 662 | 299 | 932 | 0 |
DY272797 | 322 | 327 | 647 | 0 |
BW656828 | 260 | 17 | 276 | 0 |
EL450628 | 305 | 368 | 672 | 0 |
FC882813 | 285 | 327 | 611 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|