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CAZyme Information: ASPSYDRAFT_141971-t33_1-p1
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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 | Aspergillus sydowii | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus sydowii | |||||||||||
| CAZyme ID | ASPSYDRAFT_141971-t33_1-p1 | |||||||||||
| CAZy Family | AA4 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | ||||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH31 | 595 | 1021 | 1.5e-119 | 0.9976580796252927 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 269881 | GH31_u1 | 1.52e-171 | 614 | 918 | 1 | 304 | glycosyl hydrolase family 31 (GH31); uncharacterized subgroup. This family represents an uncharacterized GH31 enzyme subgroup found in bacteria and eukaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 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. |
| 349880 | M20_bAS | 1.53e-125 | 44 | 431 | 5 | 396 | M20 Peptidase beta-alanine synthase, an amidohydrolase. Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders. |
| 236456 | PRK09290 | 1.97e-115 | 33 | 428 | 2 | 402 | allantoate amidohydrolase; Reviewed |
| 395838 | Glyco_hydro_31 | 4.24e-110 | 595 | 1021 | 1 | 442 | Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. |
| 237250 | PRK12893 | 2.06e-108 | 33 | 439 | 5 | 412 | Zn-dependent hydrolase. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 0.0 | 1 | 1224 | 1 | 1232 | |
| 0.0 | 432 | 1226 | 8 | 805 | |
| 0.0 | 432 | 1224 | 8 | 800 | |
| 0.0 | 432 | 1224 | 8 | 800 | |
| 0.0 | 432 | 1224 | 8 | 800 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4.81e-191 | 441 | 1055 | 34 | 643 | Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_B Chain B, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_C Chain C, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_D Chain D, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_E Chain E, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_F Chain F, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJA_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJB_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_B Chain B, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_C Chain C, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_D Chain D, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_E Chain E, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_F Chain F, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363] |
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| 7.38e-190 | 441 | 1055 | 34 | 643 | Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJD_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJE_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJF_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363] |
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| 2.15e-68 | 35 | 431 | 19 | 416 | X-ray crystal structure of a putative amidohydrolase/peptidase from Burkholderia cenocepacia [Burkholderia cenocepacia J2315],4WJB_B X-ray crystal structure of a putative amidohydrolase/peptidase from Burkholderia cenocepacia [Burkholderia cenocepacia J2315],4WJB_C X-ray crystal structure of a putative amidohydrolase/peptidase from Burkholderia cenocepacia [Burkholderia cenocepacia J2315],4WJB_D X-ray crystal structure of a putative amidohydrolase/peptidase from Burkholderia cenocepacia [Burkholderia cenocepacia J2315] |
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| 1.03e-63 | 32 | 428 | 24 | 421 | Crystal structure of Amidase, hydantoinase/carbamoylase family from Burkholderia multivorans [Burkholderia multivorans ATCC 17616],5THW_B Crystal structure of Amidase, hydantoinase/carbamoylase family from Burkholderia multivorans [Burkholderia multivorans ATCC 17616],5THW_C Crystal structure of Amidase, hydantoinase/carbamoylase family from Burkholderia multivorans [Burkholderia multivorans ATCC 17616],5THW_D Crystal structure of Amidase, hydantoinase/carbamoylase family from Burkholderia multivorans [Burkholderia multivorans ATCC 17616] |
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| 1.21e-62 | 22 | 428 | 12 | 421 | Crystal structure of Amidase, hydantoinase/carbamoylase family from Burkholderia vietnamiensis [Burkholderia vietnamiensis G4],5I4M_B Crystal structure of Amidase, hydantoinase/carbamoylase family from Burkholderia vietnamiensis [Burkholderia vietnamiensis G4] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2.04e-54 | 31 | 431 | 6 | 407 | N-carbamoyl-L-amino-acid hydrolase OS=Rhizobium meliloti OX=382 GN=hyuC PE=1 SV=1 |
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| 3.06e-52 | 35 | 428 | 2 | 398 | N-carbamoyl-L-amino acid hydrolase OS=Geobacillus stearothermophilus OX=1422 GN=amaB PE=1 SV=1 |
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| 7.36e-50 | 35 | 428 | 2 | 398 | N-carbamoyl-L-amino acid hydrolase OS=Geobacillus stearothermophilus OX=1422 GN=amaB PE=1 SV=2 |
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| 1.22e-46 | 31 | 428 | 2 | 406 | N-carbamoyl-L-amino-acid hydrolase OS=Pseudomonas sp. (strain NS671) OX=29441 GN=hyuC PE=1 SV=1 |
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| 2.86e-41 | 559 | 1092 | 155 | 686 | Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 1.000054 | 0.000000 |