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Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna03754.1-v1.0-hybrid |
Family | GH31 |
Protein Properties | Length: 1174 Molecular Weight: 130074 Isoelectric Point: 5.9402 |
Chromosome | Chromosome/Scaffold: 4 Start: 25324602 End: 25334054 |
Description | alpha-xylosidase 1 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH31 | 272 | 763 | 0 |
FYFFSGTSPLAVVDQYTSFIGRPAPMPYWSLGFHQCRWGYHNLSVVEDVVENYKKAQIPLDVMWTDDDHMDVRKDFTLSPTNFPRPKLLAFLDKIHKIGM KYVVIVDPGIGINSSYGVYTRGLANDVFIKYDNEPYLAQVWPGAVHFPDFLNPKTVSWWADEVKRFHELVPVDGLWIDMNEASNFCSGKCTIPKGVQCPK PGIPGWICCLDCKNITNTRWDDPPYKINASGTQVPLGFKTIATSAYHYNGVLEYDAHSLYGFTQSIATHQGLQGIAGKRPFILSRSTYVGSGKYTAHWTG DNKGTWEDLKISISTVLNFGIFGVPMVGSDICGFYPAPTEELCNRWIEVGAFYPFSRDHANFASPRQELYQWESVAISGRNALGMRYKLLPYLYTLTYEA HISGAPIARPLFFSFPTYTECYGLSTQFLLGSGLMISPVLEEGKTEVKALFPPGSWYSLFDMTQAVNSKGQYVTLDAPLHVVNVHLYQNNIL |
Full Sequence |
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Protein Sequence Length: 1174 Download |
MWSSTTTLCL SSLLILVLSL SFSGAYSYTN PKIIGKGYRL ISVEETPDGG ILGLLQLKYK 60 SKTFGPDIPL LQLFVKHETD QRLRVHITDA QKQRWEVPYN LLPREQPPSL KQSIGKAKDP 120 ITVSEYSSSE LIFSYTADPF GFVVKRKMDK QVLFDTSSDA SGPYGEMVFK DQYLEISTKL 180 PKDASLYGLG ENSQPHGIKL YPNDPYTLYT TDTSAINLNT DLYGSHPVYM DLRNVGGEAF 240 AHAVLLLNSN GMDLFYRGDS LTYKVIGGVF DFYFFSGTSP LAVVDQYTSF IGRPAPMPYW 300 SLGFHQCRWG YHNLSVVEDV VENYKKAQIP LDVMWTDDDH MDVRKDFTLS PTNFPRPKLL 360 AFLDKIHKIG MKYVVIVDPG IGINSSYGVY TRGLANDVFI KYDNEPYLAQ VWPGAVHFPD 420 FLNPKTVSWW ADEVKRFHEL VPVDGLWIDM NEASNFCSGK CTIPKGVQCP KPGIPGWICC 480 LDCKNITNTR WDDPPYKINA SGTQVPLGFK TIATSAYHYN GVLEYDAHSL YGFTQSIATH 540 QGLQGIAGKR PFILSRSTYV GSGKYTAHWT GDNKGTWEDL KISISTVLNF GIFGVPMVGS 600 DICGFYPAPT EELCNRWIEV GAFYPFSRDH ANFASPRQEL YQWESVAISG RNALGMRYKL 660 LPYLYTLTYE AHISGAPIAR PLFFSFPTYT ECYGLSTQFL LGSGLMISPV LEEGKTEVKA 720 LFPPGSWYSL FDMTQAVNSK GQYVTLDAPL HVVNVHLYQN NILPMQQGGM VSKDARMTPF 780 SLVVTFPAGA SNATAKGNIF IDDDELPDMT LGNGYSTYVD LYATLSQGSV KVWSEVQEGK 840 FALEQGLIIE KVSVLGLDGS GGASALEVDG TTVTSVSKIE LSTLEQEYQE EVEDGESKTK 900 SVMVQVNGLS LPVGKNFAMS WKMGVQGCPR VVLSLEETPG KTAFWRESGG WCPPFWRETE 960 AKAASSGPLR SICPSSCPHS LWKNDFEPSD QATKENEKRR RLGFDEVGLI IIPSAPRFRL 1020 IAPTYYVAYA LNAFRQEREG LCLGWVTRAA LKGSDIVTLY GDDAEEGHEL ALFGLLMFPL 1080 ALSSKNLSNM LYRGVYGVKL STTIDAGLHG ALSESLLGPL GDSEAERMST EKGDMRLHES 1140 GNLIDSIGLK SLRHRHGLTC GLNENMLGCR GAY* 1200 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06602 | GH31_MGAM_SI_GAA | 6.0e-89 | 292 | 456 | 169 | + 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 | 1.0e-92 | 292 | 675 | 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. | ||
cd06604 | GH31_glucosidase_II_MalA | 6.0e-106 | 292 | 675 | 393 | + 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 | 3.0e-109 | 40 | 851 | 843 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
pfam01055 | Glyco_hydro_31 | 6.0e-177 | 273 | 763 | 496 | + Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
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 | 9 | 857 | 13 | 851 | A Chain A, Crystal Structure Of A Native Endo Beta-1,3-Glucanase (Hev B 2), A Major Allergen From Hevea Brasiliensis |
PDB | 3w37_A | 0 | 9 | 857 | 13 | 851 | A Chain A, Crystal Structure Of A Native Endo Beta-1,3-Glucanase (Hev B 2), A Major Allergen From Hevea Brasiliensis |
PDB | 3lpp_D | 0 | 64 | 921 | 106 | 898 | A Chain A, Crystal Structure Of A Native Endo Beta-1,3-Glucanase (Hev B 2), A Major Allergen From Hevea Brasiliensis |
PDB | 3lpp_C | 0 | 64 | 921 | 106 | 898 | A Chain A, Crystal Structure Of A Native Endo Beta-1,3-Glucanase (Hev B 2), A Major Allergen From Hevea Brasiliensis |
PDB | 3lpp_B | 0 | 64 | 921 | 106 | 898 | A Chain A, Crystal Structure Of A Native Endo Beta-1,3-Glucanase (Hev B 2), A Major Allergen From Hevea Brasiliensis |