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CAZyme Information: OAG25730.1

You are here: Home > Sequence: OAG25730.1

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 Alternaria alternata
Lineage Ascomycota; Dothideomycetes; ; Pleosporaceae; Alternaria; Alternaria alternata
CAZyme ID OAG25730.1
CAZy Family GT32
CAZyme Description PX domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A177E2U2]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1119 KV441469|CGC7 125137.25 5.5421
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AalternataSRC1lrK2f 13577 N/A 111 13466
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.37:21 3.2.1.55:3 3.2.1.-:1 -

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH43 603 875 4.6e-134 0.9315068493150684
CBM91 903 1110 1.8e-44 0.97

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
350114 GH43_SXA-like 0.0 605 877 20 292
Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA. This glycosyl hydrolase family 43 (GH43) includes enzymes that have been characterized to mainly have beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium (Xsa;Sxa;SXA), Bifidobacterium adolescentis ATCC 15703 (XylC;XynB;BAD_0428) and Bacillus sp. KK-1 XylB. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. These enzymes possess an additional C-terminal beta-sandwich domain that restricts access for substrates to a portion of the active site to form a pocket. The active-site pockets comprise of two subsites, with binding capacity for two monosaccharide moieties and a single route of access for small molecules such as substrate. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
226038 XynB2 6.01e-162 605 1107 42 546
Beta-xylosidase [Carbohydrate transport and metabolism].
401313 Vps5 1.12e-104 353 565 1 219
Vps5 C terminal like. Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.
350103 GH43_XYL-like 1.38e-104 605 870 20 272
Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium beta-D-xylosidase SXA. These are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. It also includes various GH43 family GH43 arabinofuranosidases (EC 3.2.1.55) including Humicola insolens alpha-L-arabinofuranosidase AXHd3, Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB), and the bifunctional Phanerochaete chrysosporium xylosidase/arabinofuranosidase (Xyl;PcXyl). GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
350129 GH43_XynB-like 9.00e-101 605 877 20 285
Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB). This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been characterized to have alpha-L-arabinofuranosidase (EC 3.2.1.55) and beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activities. Beta-1,4-xylosidases are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Also included in this subfamily are Bacteroides ovatus alpha-L-arabinofuranosidases, BoGH43A and BoGH43B, both having a two-domain architecture, consisting of an N-terminal 5-bladed beta-propeller domain harboring the catalytic active site, and a C-terminal beta-sandwich domain. However, despite significant functional overlap between these two enzymes, BoGH43A and BoGH43B share just 41% sequence identity. The latter appears to be significantly less active on the same substrates, suggesting that these paralogs may play subtly different roles during the degradation of xyloglucans from different sources, or may function most optimally at different stages in the catabolism of xyloglucan oligosaccharides (XyGOs), for example before or after hydrolysis of certain side-chain moieties. It also includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a bifunctional xylosidase/arabinofuranosidase. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 600 1118 40 557
0.0 604 1113 24 533
0.0 604 1113 24 533
0.0 604 1119 24 537
0.0 604 1119 24 537

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.87e-186 205 565 1 368
Chain A, Putative vacuolar protein sorting-associated protein [Thermochaetoides thermophila DSM 1495],6H7W_B Chain B, Putative vacuolar protein sorting-associated protein [Thermochaetoides thermophila DSM 1495],6H7W_E Chain E, Putative vacuolar protein sorting-associated protein [Thermochaetoides thermophila DSM 1495],6H7W_F Chain F, Putative vacuolar protein sorting-associated protein [Thermochaetoides thermophila DSM 1495],6H7W_G Chain G, Putative vacuolar protein sorting-associated protein [Thermochaetoides thermophila DSM 1495],6H7W_H Chain H, Putative vacuolar protein sorting-associated protein [Thermochaetoides thermophila DSM 1495],6H7W_N Chain N, Putative vacuolar protein sorting-associated protein [Thermochaetoides thermophila DSM 1495],6H7W_P Chain P, Putative vacuolar protein sorting-associated protein [Thermochaetoides thermophila DSM 1495]
1.59e-148 604 1107 25 523
Chain A, xylan beta-1,4-xylosidase [Halalkalibacterium halodurans C-125],1YRZ_B Chain B, xylan beta-1,4-xylosidase [Halalkalibacterium halodurans C-125]
7.95e-143 604 1107 24 532
Chain A, beta-D-xylosidase [Geobacillus stearothermophilus],2EXI_B Chain B, beta-D-xylosidase [Geobacillus stearothermophilus],2EXI_C Chain C, beta-D-xylosidase [Geobacillus stearothermophilus],2EXI_D Chain D, beta-D-xylosidase [Geobacillus stearothermophilus]
7.95e-143 604 1107 24 532
Structure of the family43 beta-Xylosidase from geobacillus stearothermophilus [Geobacillus stearothermophilus],2EXH_B Structure of the family43 beta-Xylosidase from geobacillus stearothermophilus [Geobacillus stearothermophilus],2EXH_C Structure of the family43 beta-Xylosidase from geobacillus stearothermophilus [Geobacillus stearothermophilus],2EXH_D Structure of the family43 beta-Xylosidase from geobacillus stearothermophilus [Geobacillus stearothermophilus]
8.51e-142 604 1107 24 532
Chain A, beta-D-xylosidase [Geobacillus stearothermophilus],2EXJ_B Chain B, beta-D-xylosidase [Geobacillus stearothermophilus],2EXJ_C Chain C, beta-D-xylosidase [Geobacillus stearothermophilus],2EXJ_D Chain D, beta-D-xylosidase [Geobacillus stearothermophilus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.54e-133 604 1107 23 530
Beta-xylosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=xynB PE=1 SV=2
1.42e-132 604 1107 23 530
Beta-xylosidase OS=Bacillus pumilus OX=1408 GN=xynB PE=1 SV=2
4.44e-123 604 1107 25 532
Xylan 1,3-beta-xylosidase OS=Vibrio sp. OX=678 GN=xloA PE=1 SV=1
1.98e-119 604 1110 23 536
Putative beta-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yagH PE=3 SV=1
3.80e-68 209 565 202 576
Vacuolar protein sorting-associated protein vps5 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=vps5 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

TMHMM  Annotations      help

There is no transmembrane helices in OAG25730.1.