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CAZyme Information: FOXG_02663-t26_1-p1

You are here: Home > Sequence: FOXG_02663-t26_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Fusarium oxysporum
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
CAZyme ID FOXG_02663-t26_1-p1
CAZy Family AA7
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
573 65193.48 5.4664
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Foxysporum4287 21354 426428 429 20925
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in FOXG_02663-t26_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH31 292 533 3e-39 0.4707259953161593

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269888 GH31_MGAM_SI_GAA 1.35e-75 308 494 1 180
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase. This subgroup 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).
395838 Glyco_hydro_31 2.07e-49 292 496 5 199
Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
407105 NtCtMGAM_N 4.17e-37 69 187 1 110
N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase. NtCtMGAM_N is a beta-barrel-like structure just N-terminal to the catalytic domain of maltase-glucoamylase in eukaryotes. It contributes to the architecture of the substrate-binding site, by donating a loop that comes into close contact with two regions in the catalytic domain thereby creating the site. This family is frequently found at the N-terminus of Glycosyl hydrolase 31, pfam01055.to which it contributes as above.
224418 YicI 1.23e-32 55 487 27 426
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
269890 GH31_glucosidase_II_MalA 2.46e-31 308 478 1 161
Alpha-glucosidase II-like. 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 subgroup also includes the MalA alpha-glucosidase from Sulfolobus solfataricus 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 572 1 572
0.0 1 572 1 540
0.0 1 572 1 540
0.0 1 572 1 516
0.0 1 572 1 506

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.90e-59 57 497 44 494
Sugar beet alpha-glucosidase with acarbose [Beta vulgaris],3W38_A Sugar beet alpha-glucosidase [Beta vulgaris],3WEL_A Sugar beet alpha-glucosidase with acarviosyl-maltotriose [Beta vulgaris],3WEM_A Sugar beet alpha-glucosidase with acarviosyl-maltotetraose [Beta vulgaris],3WEN_A Sugar beet alpha-glucosidase with acarviosyl-maltopentaose [Beta vulgaris],3WEO_A Sugar beet alpha-glucosidase with acarviosyl-maltohexaose [Beta vulgaris]
2.84e-52 52 503 52 472
Crystal structure of human GAA [Homo sapiens],5KZX_A Crystal structure of human GAA [Homo sapiens]
3.78e-52 79 503 73 475
Crystral Structure of the N-terminal Subunit of Human Maltase-Glucoamylase [Homo sapiens],2QMJ_A Crystral Structure of the N-terminal Subunit of Human Maltase-Glucoamylase in Complex with Acarbose [Homo sapiens],3CTT_A Crystal complex of N-terminal Human Maltase-Glucoamylase with Casuarine [Homo sapiens]
3.90e-52 79 503 73 475
Crystal complex of N-terminal Human Maltase-Glucoamylase with BJ2661 [Homo sapiens],3L4U_A Crystal complex of N-terminal Human Maltase-Glucoamylase with de-O-sulfonated kotalanol [Homo sapiens],3L4V_A Crystal complex of N-terminal Human Maltase-Glucoamylase with kotalanol [Homo sapiens],3L4W_A Crystal complex of N-terminal Human Maltase-Glucoamylase with miglitol [Homo sapiens],3L4X_A Crystal complex of N-terminal Human Maltase-Glucoamylase with NR4-8 [Homo sapiens],3L4Y_A Crystal complex of N-terminal Human Maltase-Glucoamylase with NR4-8II [Homo sapiens],3L4Z_A Crystal complex of N-terminal Human Maltase-Glucoamylase with Salacinol [Homo sapiens]
5.21e-52 52 503 50 470
Crystal structure of human lysosomal acid-alpha-glucosidase, GAA [Homo sapiens],5NN5_A Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with 1-deoxynojirimycin [Homo sapiens],5NN6_A Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with N-hydroxyethyl-1-deoxynojirimycin [Homo sapiens],5NN8_A Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with acarbose [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.13e-144 19 572 27 586
Alpha-glucosidase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=agdA PE=2 SV=1
7.93e-141 18 572 22 585
Alpha-glucosidase OS=Aspergillus niger OX=5061 GN=aglA PE=1 SV=1
1.71e-117 27 572 43 595
Uncharacterized family 31 glucosidase C1039.11c OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC1039.11c PE=3 SV=1
9.16e-117 12 572 17 554
Glucoamylase 1 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=GAM1 PE=1 SV=3
3.31e-106 55 572 60 573
Alpha-glucosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=agl1 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000245 0.999736 CS pos: 17-18. Pr: 0.9797

TMHMM  Annotations      help

There is no transmembrane helices in FOXG_02663-t26_1-p1.