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CAZyme Information: ASPVEDRAFT_122979-t33_1-p1

You are here: Home > Sequence: ASPVEDRAFT_122979-t33_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 Aspergillus versicolor
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus versicolor
CAZyme ID ASPVEDRAFT_122979-t33_1-p1
CAZy Family AA3
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1217 135991.72 6.2668
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AversicolorCBS583.65 13364 1036611 142 13222
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in ASPVEDRAFT_122979-t33_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH31 587 1013 4.5e-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 1.30e-166 606 910 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 2.03e-127 45 432 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 8.24e-119 34 429 2 402
allantoate amidohydrolase; Reviewed
237250 PRK12893 3.04e-110 34 433 5 405
Zn-dependent hydrolase.
395838 Glyco_hydro_31 1.30e-105 587 1013 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 1216 1 1232
0.0 433 1217 16 804
0.0 433 1217 16 801
0.0 433 1217 16 801
0.0 433 1217 16 801

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.48e-192 434 1052 34 646
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]
3.81e-191 434 1052 34 646
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]
5.60e-71 36 439 19 422
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]
5.30e-66 33 434 24 426
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]
1.59e-64 33 415 24 407
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
4.97e-55 36 429 2 398
N-carbamoyl-L-amino acid hydrolase OS=Geobacillus stearothermophilus OX=1422 GN=amaB PE=1 SV=1
7.83e-53 32 434 6 409
N-carbamoyl-L-amino-acid hydrolase OS=Rhizobium meliloti OX=382 GN=hyuC PE=1 SV=1
1.21e-52 36 429 2 398
N-carbamoyl-L-amino acid hydrolase OS=Geobacillus stearothermophilus OX=1422 GN=amaB PE=1 SV=2
5.50e-46 32 434 2 411
N-carbamoyl-L-amino-acid hydrolase OS=Pseudomonas sp. (strain NS671) OX=29441 GN=hyuC PE=1 SV=1
4.91e-41 53 425 34 414
Putative hydrolase MSMEG_3995/MSMEI_3903 OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=MSMEG_3995 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000046 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in ASPVEDRAFT_122979-t33_1-p1.