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CAZyme Information: MGYG000004688_01131

You are here: Home > Sequence: MGYG000004688_01131

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 CAG-873 sp900550395
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873; CAG-873 sp900550395
CAZyme ID MGYG000004688_01131
CAZy Family GH51
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
836 92476.02 5.8932
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004688 2658373 MAG Spain Europe
Gene Location Start: 12980;  End: 15490  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.55

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH51 410 782 5.9e-97 0.5650793650793651

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3534 AbfA 6.97e-38 402 582 25 173
Alpha-L-arabinofuranosidase [Carbohydrate transport and metabolism].
pfam06964 Alpha-L-AF_C 1.13e-22 675 785 22 129
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 3.82e-22 670 799 7 145
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 4.43e-04 79 166 21 130
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.
cd08984 GH43-like 0.006 43 116 77 173
Glycosyl hydrolase family 43. This glycosyl hydrolase family 43 (GH43)-like subfamily includes uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-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-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. 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. Many of the enzymes in this family 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QKJ30384.1 1.54e-279 19 834 23 860
QJD94876.1 1.23e-276 24 789 30 806
ACU63160.1 1.14e-274 24 788 24 795
BBE18431.1 1.17e-273 24 788 31 803
AXY72738.1 2.48e-273 22 789 36 815

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6ZPS_AAA 1.47e-81 235 751 2 528
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]
2VRQ_A 8.75e-16 429 832 50 491
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]
6ZT6_A 1.16e-15 429 832 50 491
ChainA, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT6_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT6_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT7_A Chain A, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT7_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT7_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus]
6ZTA_A 1.16e-15 429 832 50 491
ChainA, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZTA_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZTA_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus]
6ZT8_A 3.57e-15 429 832 50 491
ChainA, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT8_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT8_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT9_A Chain A, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT9_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT9_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P82593 8.44e-139 235 759 36 557
Extracellular exo-alpha-L-arabinofuranosidase OS=Streptomyces chartreusis OX=1969 PE=1 SV=1
Q9SG80 9.42e-89 230 829 39 633
Alpha-L-arabinofuranosidase 1 OS=Arabidopsis thaliana OX=3702 GN=ASD1 PE=1 SV=1
Q8VZR2 1.19e-79 246 751 54 551
Alpha-L-arabinofuranosidase 2 OS=Arabidopsis thaliana OX=3702 GN=ASD2 PE=2 SV=1
B8NKA3 6.91e-71 235 743 27 529
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
Q8NK90 9.34e-71 235 743 27 528
Alpha-L-arabinofuranosidase A OS=Aspergillus kawachii (strain NBRC 4308) OX=1033177 GN=abfA PE=1 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
0.001498 0.846850 0.150703 0.000395 0.000265 0.000239

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004688_01131.