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Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.011G154200.1 |
Family | GH31 |
Protein Properties | Length: 923 Molecular Weight: 103737 Isoelectric Point: 7.5826 |
Chromosome | Chromosome/Scaffold: 11 Start: 17282311 End: 17286827 |
Description | Glycosyl hydrolases family 31 protein |
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 | 308 | 775 | 0 |
YFFAGPSPDMVIEQYTELIGRPAPMPYWSFGFHQCRYGYKNISDVEGVVAGYAKARIPLEVMWTDIDYMDAYKDFTFHPVNFPLEKMKKFVNTLHQNGQK YVVILDPGISVNSTYETYIRGMQADIFIKRNGIPYMGEVWPGKVYFPDFINPAGREFWGNEIKIFRELLPVDGLWIDMNEISNFIDPTPTPFSTVDDPPY RINNAGIRRPINNKTVPATSLHFDVMKEYNVHNLYGLLESKATNVGLINSTGKRPFVLSRSTFIGSGRYTAHWTGDNAATWDDLAYTIPSILNFGLFGIP MVGADICGFSGNTNEELCRRWIQLGSFYPFARDHSSIDTTRQELYLWDSVAASARKVLGLRYQLLPYFYTLMYEAHIKGTPIARPLFFSFPQDIKTYEVN SQFLIGKGVMVSPVLKSGATSVDAYFPAGNWFDLFNYSNTVSVSPGKYIKLAAPADHINVHVHEGNIL |
Full Sequence |
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Protein Sequence Length: 923 Download |
MPLTDHMTQK MEKERNKNSC RNTKATSPSQ SNLQLLVLLL VCGVLLTSGK DVKEEVVGYG 60 YKIGSVNSGL AGKLLTADLS LIKRSSVYGN DIQHLNLIAE FETKNRLRVR ITDSKDQRWE 120 IPQHIVPRQN HSPKNYLHYS PLNHRLLLDN NLLSDPNSDL LFTLHNTIPF GFSVTRKSSG 180 DVLFDTSTDM SNPDTFLVFK DQYIQLSSRL PIKRSSLYGL GEHTKSTFKL KPDDTFTLWN 240 ADLASANIDV NLYGSHPFYI DVRSASADGK VQAGTTHGVL LFNSNGMDIV YGGDRITYKV 300 IGGIIDLYFF AGPSPDMVIE QYTELIGRPA PMPYWSFGFH QCRYGYKNIS DVEGVVAGYA 360 KARIPLEVMW TDIDYMDAYK DFTFHPVNFP LEKMKKFVNT LHQNGQKYVV ILDPGISVNS 420 TYETYIRGMQ ADIFIKRNGI PYMGEVWPGK VYFPDFINPA GREFWGNEIK IFRELLPVDG 480 LWIDMNEISN FIDPTPTPFS TVDDPPYRIN NAGIRRPINN KTVPATSLHF DVMKEYNVHN 540 LYGLLESKAT NVGLINSTGK RPFVLSRSTF IGSGRYTAHW TGDNAATWDD LAYTIPSILN 600 FGLFGIPMVG ADICGFSGNT NEELCRRWIQ LGSFYPFARD HSSIDTTRQE LYLWDSVAAS 660 ARKVLGLRYQ LLPYFYTLMY EAHIKGTPIA RPLFFSFPQD IKTYEVNSQF LIGKGVMVSP 720 VLKSGATSVD AYFPAGNWFD LFNYSNTVSV SPGKYIKLAA PADHINVHVH EGNILALQGE 780 AMTTEEARKT AFHLLVVLSS SGNSTGELFL DDGESVEMGG ERKSWSLVKF HSEIVGDMAM 840 VRSNIINGEF AFSQKWMVSK VTFIGLKKTN GIKWYELQTS KETRSGNRRI RASLNNNGDF 900 DVLVMSGLSL FLGEEFKLNV KL* 960 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06600 | GH31_MGAM-like | 9.0e-115 | 327 | 686 | 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 | 2.0e-132 | 327 | 686 | 363 | + 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-137 | 169 | 884 | 735 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
pfam01055 | Glyco_hydro_31 | 0 | 308 | 775 | 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 | 327 | 704 | 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 | |
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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_002298949.1 | 0 | 11 | 918 | 1 | 881 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317678.1 | 0 | 11 | 922 | 1 | 912 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317679.1 | 0 | 12 | 922 | 3 | 904 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002333838.1 | 0 | 35 | 922 | 10 | 895 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002534242.1 | 0 | 55 | 922 | 39 | 912 | alpha-glucosidase, putative [Ricinus communis] |
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 | 36 | 922 | 20 | 908 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3w37_A | 0 | 36 | 922 | 20 | 908 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3ctt_A | 0 | 75 | 815 | 65 | 775 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 2qmj_A | 0 | 75 | 815 | 65 | 775 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 2qly_A | 0 | 75 | 815 | 65 | 775 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch degradation I | RXN-2141 | EC-3.2.1.20 | α-glucosidase |