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CAZyme Information: MGYG000001372_00156

You are here: Home > Sequence: MGYG000001372_00156

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 Paraprevotella xylaniphila
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Paraprevotella; Paraprevotella xylaniphila
CAZyme ID MGYG000001372_00156
CAZy Family GH51
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
861 96297.02 6.9356
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001372 3789432 Isolate not provided not provided
Gene Location Start: 28314;  End: 30899  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.55

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH51 410 859 2.2e-98 0.6952380952380952

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3534 AbfA 4.88e-39 420 778 33 290
Alpha-L-arabinofuranosidase [Carbohydrate transport and metabolism].
pfam06964 Alpha-L-AF_C 1.29e-28 674 851 1 192
Alpha-L-arabinofuranosidase C-terminal domain. This family represents the C-terminus (approximately 200 residues) of bacterial and eukaryotic alpha-L-arabinofuranosidase (EC:3.2.1.55). This catalyzes the hydrolysis of nonreducing terminal alpha-L-arabinofuranosidic linkages in L-arabinose-containing polysaccharides.
smart00813 Alpha-L-AF_C 3.45e-22 674 851 1 189
Alpha-L-arabinofuranosidase C-terminus. This entry represents the C terminus (approximately 200 residues) of bacterial and eukaryotic alpha-L-arabinofuranosidase. This catalyses the hydrolysis of non-reducing terminal alpha-L-arabinofuranosidic linkages in L-arabinose-containing polysaccharides.
cd08983 GH43_Bt3655-like 2.11e-08 81 172 21 129
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 arabinofuranosidase Bt3655. This glycosyl hydrolase family 43 (GH43)-like family includes the characterized arabinofuranosidases (EC 3.2.1.55): Bacteroides thetaiotaomicron VPI-5482 (Bt3655;BT_3655) and Penicillium chrysogenum 31B Abf43B, as well as Bifidobacterium adolescentis ATCC 15703 beta-xylosidase (EC 3.2.1.37) BAD_1527. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. 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.
pfam02018 CBM_4_9 5.60e-08 271 410 1 128
Carbohydrate binding domain. This family includes diverse carbohydrate binding domains.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QRX64621.1 0.0 1 858 1 860
SCD19721.1 0.0 20 859 27 864
AOW08962.1 0.0 22 860 29 869
AHW59500.1 0.0 20 860 18 862
QIA06585.1 0.0 20 857 18 859

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6ZPS_AAA 6.16e-82 237 855 1 622
ChainAAA, MgGH51 [Meripilus giganteus],6ZPV_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPW_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPX_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPY_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPZ_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZQ0_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZQ1_AAA Chain AAA, MgGH51 [Meripilus giganteus]
4ATW_A 1.36e-13 435 588 46 172
Thecrystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_B The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_C The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_D The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_E The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_F The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8]
3S2C_A 1.37e-13 435 588 46 172
Structureof the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_B Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_C Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_D Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_E Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_F Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_G Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_H Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_I Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_J Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_K Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_L Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1]
2VRQ_A 1.43e-13 436 589 50 177
StructureOf An Inactive Mutant Of Arabinofuranosidase From Thermobacillus Xylanilyticus In Complex With A Pentasaccharide [Thermobacillus xylanilyticus],2VRQ_B Structure Of An Inactive Mutant Of Arabinofuranosidase From Thermobacillus Xylanilyticus In Complex With A Pentasaccharide [Thermobacillus xylanilyticus],2VRQ_C Structure Of An Inactive Mutant Of Arabinofuranosidase From Thermobacillus Xylanilyticus In Complex With A Pentasaccharide [Thermobacillus xylanilyticus]
3UG3_A 1.47e-13 435 588 66 192
Crystalstructure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_B Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_C Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_D Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_E Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_F Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG4_A Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_B Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_C Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_D Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_E Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_F Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG5_A Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_B Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_C Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_D Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_E Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_F Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P82593 4.70e-133 232 777 30 566
Extracellular exo-alpha-L-arabinofuranosidase OS=Streptomyces chartreusis OX=1969 PE=1 SV=1
Q9SG80 1.10e-82 232 761 38 552
Alpha-L-arabinofuranosidase 1 OS=Arabidopsis thaliana OX=3702 GN=ASD1 PE=1 SV=1
Q8VZR2 1.76e-77 238 761 48 551
Alpha-L-arabinofuranosidase 2 OS=Arabidopsis thaliana OX=3702 GN=ASD2 PE=2 SV=1
Q0CTV2 6.14e-76 233 754 24 529
Probable alpha-L-arabinofuranosidase A OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=abfA PE=3 SV=1
B8NKA3 5.51e-72 230 754 19 530
Probable alpha-L-arabinofuranosidase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=abfA PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000365 0.998845 0.000248 0.000173 0.000166 0.000153

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001372_00156.