| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G034575_T03 |
| Family | GH31 |
| Protein Properties | Length: 559 Molecular Weight: 62837.4 Isoelectric Point: 8.6974 |
| Chromosome | Chromosome/Scaffold: 9 Start: 146533570 End: 146540053 |
| Description | Glycosyl hydrolases family 31 protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH31 | 106 | 417 | 0 |
| TATPCWPGSSSYPDMLNPEIREWWADKFSYENYKGSTPTLYIWNDMNEPSVFNGPEVTMPRDAMHYGDVEHRELHNAYGYYFHMATADGLLKRDKGKHRP FVLSRAFFAGSQRYGAVWTGDNSADWDHLKSSIPMVLILGLTGLPFSGADVGGFFGNPEPDLLVRWYQVGAFYPFFRGHAHHDTKRREPWLFGERRTAII REAIHMRYSLLPYFYTLFREASVNGIPVMRPLWLEFPEDKETYNNGEAFMVGPSLLAQGIYEEGQKSVSVYLPGKESWYDLRNGSPYKGSVTHKLQVLED SIPSFQRAGTIV | |||
| Full Sequence |
|---|
| Protein Sequence Length: 559 Download |
| MDPPPRRLAA PLLLLLLAAA SPAARAWKKD EFRNCNQTPF CKRARTRAPH SLEAPLSLAA 60 GSLAVSPDGS ISAELSHPSR PRPLVLRLSV LPPHALRLQI DEDYSTATPC WPGSSSYPDM 120 LNPEIREWWA DKFSYENYKG STPTLYIWND MNEPSVFNGP EVTMPRDAMH YGDVEHRELH 180 NAYGYYFHMA TADGLLKRDK GKHRPFVLSR AFFAGSQRYG AVWTGDNSAD WDHLKSSIPM 240 VLILGLTGLP FSGADVGGFF GNPEPDLLVR WYQVGAFYPF FRGHAHHDTK RREPWLFGER 300 RTAIIREAIH MRYSLLPYFY TLFREASVNG IPVMRPLWLE FPEDKETYNN GEAFMVGPSL 360 LAQGIYEEGQ KSVSVYLPGK ESWYDLRNGS PYKGSVTHKL QVLEDSIPSF QRAGTIVPRK 420 DRFRRSSTQM VNDPYTLVIA LNSSGAAEGE LYMDDGKSYD YQQGAFSHRR FVFADNKLTS 480 FNIAPDNLSK KFTSGCVIER IIVLGLRSGV KKAIIEPGNQ EVEIESGPIS LRSGSSPVVP 540 TIRRPNVRIA DSWTIWIA* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd06600 | GH31_MGAM-like | 3.0e-88 | 110 | 330 | 221 | + 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 | 9.0e-110 | 109 | 330 | 229 | + 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-123 | 109 | 480 | 374 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
| pfam01055 | Glyco_hydro_31 | 2.0e-140 | 110 | 417 | 313 | + Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. | ||
| cd06603 | GH31_GANC_GANAB_alpha | 2.0e-160 | 110 | 330 | 221 | + 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. | ||
| 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 | ACN26464.1 | 0 | 110 | 558 | 283 | 731 | unknown [Zea mays] |
| GenBank | ACN34619.1 | 1.4013e-45 | 1 | 125 | 1 | 126 | unknown [Zea mays] |
| GenBank | ACN34619.1 | 0 | 110 | 558 | 469 | 917 | unknown [Zea mays] |
| RefSeq | XP_002468270.1 | 8.99998e-41 | 1 | 125 | 1 | 126 | hypothetical protein SORBIDRAFT_01g042750 [Sorghum bicolor] |
| RefSeq | XP_002468270.1 | 0 | 110 | 558 | 469 | 917 | hypothetical protein SORBIDRAFT_01g042750 [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 | 110 | 535 | 431 | 880 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
| PDB | 3w37_A | 0 | 110 | 535 | 431 | 880 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
| PDB | 3lpp_D | 0 | 111 | 526 | 435 | 870 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
| PDB | 3lpp_C | 0 | 111 | 526 | 435 | 870 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
| PDB | 3lpp_B | 0 | 111 | 526 | 435 | 870 | A Chain A, Crystral Structure Of The N-Terminal Subunit Of Human Maltase- Glucoamylase |
