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CAZyme Information: MGYG000001512_03215

You are here: Home > Sequence: MGYG000001512_03215

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 Coprobacter secundus
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Coprobacteraceae; Coprobacter; Coprobacter secundus
CAZyme ID MGYG000001512_03215
CAZy Family GH43
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1306 MGYG000001512_19|CGC34 146818.66 6.3783
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001512 4253015 Isolate not provided not provided
Gene Location Start: 1551018;  End: 1554938  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001512_03215.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH127 534 1076 4.2e-209 0.9980916030534351
GH43 30 312 1.1e-127 0.99644128113879

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07944 Glyco_hydro_127 2.57e-175 533 1076 1 503
Beta-L-arabinofuranosidase, GH127. One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.
COG3533 COG3533 5.45e-166 540 1160 22 589
Uncharacterized conserved protein, DUF1680 family [Function unknown].
cd08999 GH43_ABN-like 7.49e-105 30 313 1 284
Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) 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. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. 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.
pfam04616 Glyco_hydro_43 7.23e-71 30 312 3 281
Glycosyl hydrolases family 43. The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyze the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
cd08991 GH43_HoAraf43-like 9.04e-55 38 310 1 276
Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580). This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT86297.1 0.0 516 1306 19 807
AND18710.1 0.0 516 1306 19 807
QJR78611.1 0.0 516 1306 19 807
AII66951.1 0.0 516 1306 15 803
ALA72775.1 0.0 516 1306 15 803

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6EX6_A 7.13e-220 524 1181 5 648
TheGH127, Beta-arabinofuranosidase, BT3674 [Bacteroides thetaiotaomicron VPI-5482],6EX6_B The GH127, Beta-arabinofuranosidase, BT3674 [Bacteroides thetaiotaomicron VPI-5482]
4QJY_A 1.74e-159 532 1155 14 644
Crystalstructure of native Ara127N, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QJY_B Crystal structure of native Ara127N, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus]
4QK0_A 2.30e-154 532 1155 14 644
Crystalstructure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QK0_B Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QK0_C Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QK0_D Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus]
5MQO_A 1.27e-118 534 1157 44 695
Glycosidehydrolase BT_1003 [Bacteroides thetaiotaomicron]
3WRE_A 2.70e-111 533 1155 2 655
Thecrystal structure of native HypBA1 from Bifidobacterium longum JCM 1217 [Bifidobacterium longum subsp. longum JCM 1217],3WRG_A The complex structure of HypBA1 with L-arabinose [Bifidobacterium longum subsp. longum JCM 1217]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
E8MGH8 1.48e-110 533 1155 2 655
Non-reducing end beta-L-arabinofuranosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA1 PE=1 SV=1
A9ZND1 1.20e-28 30 313 7 308
Xylan 1,3-beta-xylosidase OS=Vibrio sp. OX=678 GN=xloA PE=1 SV=1
P45982 4.36e-26 30 312 6 291
Xylosidase/arabinosidase OS=Butyrivibrio fibrisolvens OX=831 GN=xylB PE=3 SV=1
P94489 1.60e-25 30 313 5 302
Beta-xylosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=xynB PE=1 SV=2
P07129 4.88e-22 30 313 5 302
Beta-xylosidase OS=Bacillus pumilus OX=1408 GN=xynB 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
0.000315 0.998994 0.000195 0.000168 0.000155 0.000147

TMHMM  Annotations      download full data without filtering help

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