logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002561_03378

You are here: Home > Sequence: MGYG000002561_03378

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 Bacteroides sp902388495
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp902388495
CAZyme ID MGYG000002561_03378
CAZy Family GH43
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
666 MGYG000002561_41|CGC1 75971.06 6.0191
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002561 4554549 MAG China Asia
Gene Location Start: 10387;  End: 12387  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002561_03378.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH43 21 304 2.2e-115 0.9966555183946488
GH76 323 625 4.7e-80 0.8491620111731844

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd18616 GH43_ABN-like 9.05e-161 23 299 1 291
Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activity. 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. 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 8.46e-87 21 304 1 281
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.
cd08998 GH43_Arb43a-like 2.14e-84 32 299 3 277
Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 endo-alpha-1,5-L-arabinanase Arb43A. This glycosyl hydrolase family 43 (GH43) subgroup 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. 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. Many of these enzymes such as the Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. 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.
cd08988 GH43_ABN 4.01e-72 31 299 1 277
Glycosyl hydrolase family 43. 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.
cd08999 GH43_ABN-like 1.00e-64 23 305 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QCQ48882.1 1.52e-223 322 655 35 368
QCQ44369.1 1.52e-223 322 655 35 368
QTO26877.1 1.52e-223 322 655 35 368
QLK81763.1 1.52e-223 322 655 35 368
AUI48766.1 2.15e-223 322 655 35 368

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4BOK_A 8.53e-53 328 646 10 332
ChainA, Alpha-1,6-mannanase [Niallia circulans]
4BOJ_A 1.28e-52 328 646 13 335
ChainA, Alpha-1,6-mannanase [Niallia circulans],4BOJ_B Chain B, Alpha-1,6-mannanase [Niallia circulans],4BOJ_C Chain C, Alpha-1,6-mannanase [Niallia circulans]
4D4A_A 2.83e-52 318 646 21 353
ChainA, Alpha-1,6-mannanase [Niallia circulans],4D4A_B Chain B, Alpha-1,6-mannanase [Niallia circulans],4D4B_A Chain A, Alpha-1,6-mannanase [Niallia circulans],4D4B_B Chain B, Alpha-1,6-mannanase [Niallia circulans],4D4C_A Chain A, Alpha-1,6-mannanase [Niallia circulans],4D4C_B Chain B, Alpha-1,6-mannanase [Niallia circulans],4D4D_A Chain A, Alpha-1,6-mannanase [Niallia circulans],4D4D_B Chain B, Alpha-1,6-mannanase [Niallia circulans],5N0F_A Chain A, Alpha-1,6-mannanase [Niallia circulans],5N0F_B Chain B, Alpha-1,6-mannanase [Niallia circulans],6ZBX_A Chain A, Alpha-1,6-mannanase [Niallia circulans],6ZBX_B Chain B, Alpha-1,6-mannanase [Niallia circulans],7NL5_A Chain A, Alpha-1,6-mannanase [Niallia circulans]
5AGD_A 1.44e-51 318 646 21 353
ChainA, Alpha-1,6-mannanase [Niallia circulans],5AGD_B Chain B, Alpha-1,6-mannanase [Niallia circulans],6ZBM_A Chain A, Alpha-1,6-mannanase [Niallia circulans],6ZBW_A Chain A, Alpha-1,6-mannanase [Niallia circulans],6ZBW_B Chain B, Alpha-1,6-mannanase [Niallia circulans]
5M77_A 5.83e-50 328 646 44 366
ChainA, Alpha-1,6-mannanase [Niallia circulans],5M77_B Chain B, Alpha-1,6-mannanase [Niallia circulans]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P94522 4.18e-39 6 305 18 322
Extracellular endo-alpha-(1->5)-L-arabinanase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=abnA PE=1 SV=3
P95470 3.91e-36 32 306 38 333
Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=arbA PE=1 SV=1
Q2U8C6 1.30e-32 7 306 6 319
Probable arabinan endo-1,5-alpha-L-arabinosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=abnA PE=3 SV=1
B8NDL1 1.30e-32 7 306 6 319
Probable arabinan endo-1,5-alpha-L-arabinosidase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=abnA PE=3 SV=1
Q93HT9 7.33e-32 32 304 27 311
Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus thermodenitrificans OX=33940 GN=abn-ts PE=1 SV=1

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
0.000285 0.999012 0.000180 0.000180 0.000165 0.000148

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002561_03378.