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CAZyme Information: FOIG_12688-t36_1-p1

You are here: Home > Sequence: FOIG_12688-t36_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 odoratissimum
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium odoratissimum
CAZyme ID FOIG_12688-t36_1-p1
CAZy Family GH5
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
549 58412.24 6.4917
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_FodoratissimumNRRL54006 16975 1089451 341 16634
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.22:1 3.2.1.88:1 3.2.1.22:1 3.2.1.88:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 131 379 8.5e-60 0.9737991266375546

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269893 GH27 7.34e-100 26 315 1 271
glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
178295 PLN02692 2.05e-69 25 379 55 385
alpha-galactosidase
166449 PLN02808 1.89e-67 25 393 31 376
alpha-galactosidase
177874 PLN02229 1.92e-66 25 393 62 410
alpha-galactosidase
374582 Melibiase_2 1.84e-47 25 315 1 284
Alpha galactosidase A.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 549 1 549
0.0 1 549 1 549
0.0 1 549 1 551
0.0 1 549 1 551
0.0 1 549 1 551

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.83e-57 25 379 8 338
Nicotiana benthamiana alpha-galactosidase [Nicotiana benthamiana]
2.86e-56 25 393 8 352
Chain A, alpha-galactosidase [Oryza sativa]
3.83e-53 25 379 8 368
Crystal structure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea]
1.21e-49 26 398 12 408
Chain A, alpha-galactosidase [Trichoderma reesei],1T0O_A Chain A, alpha-galactosidase [Trichoderma reesei]
7.01e-44 25 385 29 407
Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRL_A Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.71e-74 7 406 15 407
Probable alpha-galactosidase D OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=aglD PE=3 SV=2
8.24e-71 25 400 30 400
Probable alpha-galactosidase D OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=aglD PE=3 SV=2
8.24e-71 25 400 30 400
Probable alpha-galactosidase D OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=aglD PE=3 SV=2
6.04e-70 5 400 12 400
Probable alpha-galactosidase D OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=aglD PE=3 SV=1
1.95e-65 25 400 33 397
Probable alpha-galactosidase D OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=aglD PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000224 0.999736 CS pos: 19-20. Pr: 0.9774

TMHMM  Annotations      help

There is no transmembrane helices in FOIG_12688-t36_1-p1.