Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 142083 |
Family | GH31 |
Protein Properties | Length: 824 Molecular Weight: 93136.7 Isoelectric Point: 6.3417 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH31 | 236 | 678 | 0 |
FVFVGPGPKDVVQQYTGVTGTTAMPPFFSIGYHQCRWNYKDEADVAQVDAKFDEYDIPYDVIWLDIEHTDGKRYFTWDPITFPTPKEMQAKLEAKGRHMV AIVDPHIKRDEGFALHKEATSKGYYVKNSHGSDYDGWCWPGSSSYPDLVNPEIRAWWAEKFTLKNYVGSTSILHIWNDMNEPSVFNGPEVSMPRDNLHYN GIEHRDVHNAYGYYFHMATTQGLRNREGQRPFVLSRAVFAGTQKIGPIWTGDNTADWEQLRVSVPMILSLGITGIAFTGADVGGFFGNPSSELLTRWYQL GAFYPFFRAHAHLDTKRREPWIPGEPYTSRIREAIHTRYALLPYYYTLFREAHETGIPVMRPLWFEHPNDPETFAMDDEFLIGDALLVRSVYTEGSNLET VYLPGSEPWFDIKTGQSFNGGKTYKLAVSQDSIPAFQRGGTII |
Full Sequence |
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Protein Sequence Length: 824 Download |
MVYQGGVLRI KVDQENVPGG KKRFEVPDVL VDGLEKKRLW LQRITAKDGL STFYLSSGHE 60 VVLQHEPFQV YVTRGQEKLV SVNGKGLFHF EQRREKQEGE NWEEHFRSHT DSRPYGPQSI 120 GFDVSFHGAE HVYGIPERAT SLALKPTRGT EEHSEPYRLF NLDVFEYLAE SPFGLYGSIP 180 FMLSHGSKRT SGFFWLNAAE MLIDVLSPGW DGAAGEESKQ GIDTHWFAEA GIVDAFVFVG 240 PGPKDVVQQY TGVTGTTAMP PFFSIGYHQC RWNYKDEADV AQVDAKFDEY DIPYDVIWLD 300 IEHTDGKRYF TWDPITFPTP KEMQAKLEAK GRHMVAIVDP HIKRDEGFAL HKEATSKGYY 360 VKNSHGSDYD GWCWPGSSSY PDLVNPEIRA WWAEKFTLKN YVGSTSILHI WNDMNEPSVF 420 NGPEVSMPRD NLHYNGIEHR DVHNAYGYYF HMATTQGLRN REGQRPFVLS RAVFAGTQKI 480 GPIWTGDNTA DWEQLRVSVP MILSLGITGI AFTGADVGGF FGNPSSELLT RWYQLGAFYP 540 FFRAHAHLDT KRREPWIPGE PYTSRIREAI HTRYALLPYY YTLFREAHET GIPVMRPLWF 600 EHPNDPETFA MDDEFLIGDA LLVRSVYTEG SNLETVYLPG SEPWFDIKTG QSFNGGKTYK 660 LAVSQDSIPA FQRGGTIIPR KDRFRRSSSQ MVDDPYTLVI ALNSTQEAQG ELYIDDGKSY 720 EFEKGAFIHR RFSFSGGKLS SSSASPASKS YKTLSTVERI IILGLDAKKV PAAHRALVEE 780 GGQDRQADIE AAPPVLRAKL KSNAVAVRLP NVSIDKDWSI KVL* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06600 | GH31_MGAM-like | 6.0e-131 | 258 | 591 | 335 | + 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 | 1.0e-152 | 258 | 591 | 339 | + 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. | ||
cd06603 | GH31_GANC_GANAB_alpha | 0 | 258 | 591 | 336 | + This family includes the closely related glycosyl hydrolase family 31 (GH31) isozymes, neutral alpha-glucosidase C (GANC) and the alpha subunit of heterodimeric neutral alpha-glucosidase AB (GANAB). Initially distinguished on the basis of differences in electrophoretic mobility in starch gel, GANC and GANAB have been shown to have other differences, including those of substrate specificity. 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. The GANC/GANAB family includes the alpha-glucosidase II (ModA) from Dictyostelium discoideum as well as the alpha-glucosidase II (GLS2, or ROT2 - Reversal of TOR2 lethality protein 2) from Saccharomyces cerevisiae. | ||
pfam01055 | Glyco_hydro_31 | 0 | 236 | 678 | 450 | + Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. | ||
COG1501 | COG1501 | 0 | 47 | 727 | 690 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] |
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 | 131 | 768 | 206 | 854 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
PDB | 3w37_A | 0 | 131 | 768 | 206 | 854 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
PDB | 2g3n_F | 0 | 125 | 679 | 57 | 609 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
PDB | 2g3n_E | 0 | 125 | 679 | 57 | 609 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
PDB | 2g3n_D | 0 | 125 | 679 | 57 | 609 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch degradation I | RXN-2141 | EC-3.2.1.20 | α-glucosidase |
Sequence Alignments (This image is cropped. Click for full image.) |
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