y
Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.008G183500.2 |
Family | GH31 |
Protein Properties | Length: 700 Molecular Weight: 77801.9 Isoelectric Point: 7.1003 |
Chromosome | Chromosome/Scaffold: 08 Start: 46170237 End: 46175134 |
Description | alpha-xylosidase 1 |
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 | 43 | 534 | 0 |
FYFFSGPTPLGVVDQYTSFIGRPAPMPYWSLGFHQCRWGYHNLSVVEDVVENYRKAQIPLDVIWNDDDHMDGHKDFTLNPVNYPRPKLLAFLDKIHSRGM KYIVIIDPGIGVNSSYGVYQRGIANDVFIKYDGEPYLAQVWPGAVNFPDFLNPNTVAWWGDEVRRFHELVPVDGLWIDMNEASNFCSGKCTIPKGKQCPS GTGPGWICCLDCKNITKTRWDDPPYKINASGLQVPIGFKTIATSAVHYNGVLEYDAHSLYGFSQAIATHKALQGLEGKRPFILSRSTYVGSGKYAAHWTG DNKGTWEDLKYSITTVLNFGMFGVPMVGADICGFYPAPTEELCNRWIEVGAFYPFSRDHANYYSPRQELYQWKTVTKSAQNALGMRYKLLPYLYTLNYLA HTSGAPIARPLFFSFPAYKECYGLSTQFLLGSSLMVSPVLEKGKTSVKALFPPGSWYSLFDMTQTIVSKGQYFTLDAPLHVVNVHLYQNTIL |
Full Sequence |
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Protein Sequence Length: 700 Download |
MDLRNVGGQP FAHAVLLLNS NGMDVFYRGN SLTYKIIGGV FDFYFFSGPT PLGVVDQYTS 60 FIGRPAPMPY WSLGFHQCRW GYHNLSVVED VVENYRKAQI PLDVIWNDDD HMDGHKDFTL 120 NPVNYPRPKL LAFLDKIHSR GMKYIVIIDP GIGVNSSYGV YQRGIANDVF IKYDGEPYLA 180 QVWPGAVNFP DFLNPNTVAW WGDEVRRFHE LVPVDGLWID MNEASNFCSG KCTIPKGKQC 240 PSGTGPGWIC CLDCKNITKT RWDDPPYKIN ASGLQVPIGF KTIATSAVHY NGVLEYDAHS 300 LYGFSQAIAT HKALQGLEGK RPFILSRSTY VGSGKYAAHW TGDNKGTWED LKYSITTVLN 360 FGMFGVPMVG ADICGFYPAP TEELCNRWIE VGAFYPFSRD HANYYSPRQE LYQWKTVTKS 420 AQNALGMRYK LLPYLYTLNY LAHTSGAPIA RPLFFSFPAY KECYGLSTQF LLGSSLMVSP 480 VLEKGKTSVK ALFPPGSWYS LFDMTQTIVS KGQYFTLDAP LHVVNVHLYQ NTILPMQQGG 540 MISKEARMTP FTLIVTFPAG ASEAQAKGNL YLDNDELPEM KLGNGYSTHV DLYATLKQGL 600 VKIWSEVQEG KFALDKGWKI EKITVLGLSG SVDTSGLEIN GSPVANGASN IELTSVEQMH 660 LQDVEDGVGK KKSLIVSLSG LNLYVGQKFD MSMKMGVQG* 720 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam01055 | Glyco_hydro_31 | 4.0e-90 | 44 | 231 | 188 | + 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 | 3.0e-93 | 296 | 464 | 170 | + 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). | ||
cd06603 | GH31_GANC_GANAB_alpha | 2.0e-100 | 63 | 446 | 393 | + 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 | 1.0e-108 | 288 | 534 | 252 | + Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. | ||
cd06604 | GH31_glucosidase_II_MalA | 4.0e-125 | 63 | 446 | 390 | + 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. |
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 |
EMBL | CAA10382.2 | 0 | 1 | 697 | 240 | 935 | alpha-D-xylosidase [Tropaeolum majus] |
RefSeq | XP_002282429.1 | 0 | 1 | 699 | 226 | 924 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002311455.1 | 0 | 1 | 699 | 212 | 910 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002315944.1 | 0 | 1 | 699 | 230 | 928 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002531635.1 | 0 | 1 | 699 | 232 | 930 | 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 | 1 | 694 | 250 | 907 | A Chain A, Structure Of N-Myristoyltransferase From L. Donovani |
PDB | 3w37_A | 0 | 1 | 694 | 250 | 907 | A Chain A, Structure Of N-Myristoyltransferase From L. Donovani |
PDB | 3lpp_D | 0 | 1 | 674 | 249 | 896 | A Chain A, Structure Of N-Myristoyltransferase From L. Donovani |
PDB | 3lpp_C | 0 | 1 | 674 | 249 | 896 | A Chain A, Structure Of N-Myristoyltransferase From L. Donovani |
PDB | 3lpp_B | 0 | 1 | 674 | 249 | 896 | A Chain A, Structure Of N-Myristoyltransferase From L. Donovani |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO795307 | 672 | 26 | 696 | 0 |
ES818715 | 385 | 203 | 586 | 0 |
ES819167 | 382 | 311 | 690 | 0 |
CO123047 | 281 | 311 | 591 | 0 |
CO122470 | 280 | 316 | 595 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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