logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000032_05928

You are here: Home > Sequence: MGYG000000032_05928

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 Hungatella effluvii
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Hungatella; Hungatella effluvii
CAZyme ID MGYG000000032_05928
CAZy Family GH43
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
800 MGYG000000032_32|CGC1 93118.18 4.8994
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000032 6969476 Isolate United Kingdom Europe
Gene Location Start: 23478;  End: 25880  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000032_05928.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH43 12 318 3.8e-104 0.9931972789115646

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd16033 sulfatase_like 1.29e-146 328 791 1 402
uncharacterized sulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
cd18817 GH43f_LbAraf43-like 7.90e-146 20 288 1 262
Glycosyl hydrolase family 43 such as Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43. This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with alpha-L-arabinofuranosidase (EC 3.2.1.55) activity. 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 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. Characterized enzymes belonging to this subgroup include Lactobacillus brevis (LbAraf43) and Weissella sp (WAraf43) which show activity with similar catalytic efficiency on 1,5-alpha-L-arabinooligosaccharides with a degree of polymerization (DP) of 2-3; size is limited by an extended loop at the entrance to the active site. 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.
COG3940 COG3940 4.55e-124 10 320 4 310
Beta-xylosidase, GH43 family [Carbohydrate transport and metabolism].
cd08980 GH43_LbAraf43-like 4.48e-103 20 288 1 276
Glycosyl hydrolase family 43 proteins such as Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans GbtXyl43B. This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55) and possibly bifunctional xylosidase/arabinofuranosidase activities. In addition to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans IT-08 beta-xylosidase / exo-xylanase (GbtXyl43B). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) familiesGH43 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.
cd18819 GH43_LbAraf43-like 2.83e-99 20 288 1 277
Glycosyl hydrolase family 43 proteins similar to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans GbtXyl43B. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes enzymes with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55) and possibly bifunctional xylosidase/arabinofuranosidase activities, similar to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans IT-08 beta-xylosidase / exo-xylanase (GbtXyl43B). 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 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
QJU16705.1 4.77e-147 1 325 1 321
QHQ61663.1 9.86e-147 1 325 1 320
ANW98491.1 1.55e-143 1 324 1 322
AGC68110.1 1.55e-143 1 324 1 322
ANX01025.1 1.55e-143 1 324 1 322

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3K1U_A 4.63e-99 14 320 12 314
Beta-xylosidase,family 43 glycosyl hydrolase from Clostridium acetobutylicum [Clostridium acetobutylicum]
5M8E_A 4.27e-97 3 320 17 335
Crystalstructure of a GH43 arabonofuranosidase from Weissella sp. strain 142 [Weissella cibaria],5M8E_B Crystal structure of a GH43 arabonofuranosidase from Weissella sp. strain 142 [Weissella cibaria]
5M8B_A 2.48e-96 10 320 26 337
ChainA, Alpha-L-arabinofuranosidase II [Levilactobacillus brevis],5M8B_B Chain B, Alpha-L-arabinofuranosidase II [Levilactobacillus brevis]
3AKF_A 9.46e-91 14 320 14 312
Crystalstructure of exo-1,5-alpha-L-arabinofuranosidase [Streptomyces avermitilis MA-4680 = NBRC 14893],3AKG_A Crystal structure of exo-1,5-alpha-L-arabinofuranosidase complexed with alpha-1,5-L-arabinofuranobiose [Streptomyces avermitilis MA-4680 = NBRC 14893],3AKH_A Crystal structure of exo-1,5-alpha-L-arabinofuranosidase complexed with alpha-1,5-L-arabinofuranotriose [Streptomyces avermitilis MA-4680 = NBRC 14893],3AKI_A Crystal structure of exo-1,5-alpha-L-arabinofuranosidase complexed with alpha-L-arabinofuranosyl azido [Streptomyces avermitilis MA-4680 = NBRC 14893]
6PT6_A 1.80e-32 321 783 20 467
Crystalstructure of PsS1_NC C84S in complex with i-neocarratetraose [Pseudoalteromonas fuliginea],6PT6_B Crystal structure of PsS1_NC C84S in complex with i-neocarratetraose [Pseudoalteromonas fuliginea],6PT9_A Crystal structure of PsS1_NC C84S in complex with k-neocarrabiose [Pseudoalteromonas fuliginea],6PT9_B Crystal structure of PsS1_NC C84S in complex with k-neocarrabiose [Pseudoalteromonas fuliginea]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q82P90 7.53e-90 14 320 40 338
Extracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) OX=227882 GN=Araf43A PE=1 SV=1
P82594 1.56e-89 11 297 50 328
Extracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Streptomyces chartreusis OX=1969 PE=1 SV=1
G4MMH2 1.34e-71 9 320 39 344
Alpha-L-arabinofuranosidase B OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=abfB PE=1 SV=1
Q89YS5 1.51e-29 324 779 49 517
N-acetylglucosamine-6-O-sulfatase OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=BT_4656 PE=1 SV=1
P31447 6.58e-28 326 786 2 427
Uncharacterized sulfatase YidJ OS=Escherichia coli (strain K12) OX=83333 GN=yidJ PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000049 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000032_05928.