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CAZyme Information: MGYG000001666_00674

You are here: Home > Sequence: MGYG000001666_00674

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
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873;
CAZyme ID MGYG000001666_00674
CAZy Family GH30
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
533 MGYG000001666_25|CGC1 60188.82 6.6936
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001666 2832137 MAG United States North America
Gene Location Start: 91;  End: 1692  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001666_00674.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH43 240 503 5.1e-89 0.981203007518797
GH30 2 228 3.3e-65 0.45454545454545453

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd08981 GH43_Bt1873-like 3.65e-125 235 525 1 288
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron BT_1873. This glycosyl hydrolase family 43 (GH43) subfamily includes Bacteroides thetaiotaomicron VPI-5482 endo-arabinase (Bt1873;BT_1873), as well as 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 GH43 enzymes in this family may 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.
pfam04616 Glyco_hydro_43 2.44e-28 242 509 12 262
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.
pfam14587 Glyco_hydr_30_2 6.74e-28 3 99 268 367
O-Glycosyl hydrolase family 30.
cd08991 GH43_HoAraf43-like 3.41e-27 242 529 2 281
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.
cd08978 GH_F 4.57e-18 242 502 2 251
Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F. This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). 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. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. 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 of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 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
QUT89984.1 2.48e-170 233 527 31 325
QDO67471.1 3.51e-170 233 527 31 325
QCD35084.1 8.16e-170 233 527 30 324
ALJ58900.1 1.12e-166 233 527 32 326
AHW58608.1 6.93e-164 228 529 25 327

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5C0P_A 1.79e-46 233 517 19 294
Thecrystal structure of endo-arabinase from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482]
3CLW_A 2.66e-25 3 183 272 455
Crystalstructure of conserved exported protein from Bacteroides fragilis [Bacteroides fragilis NCTC 9343],3CLW_B Crystal structure of conserved exported protein from Bacteroides fragilis [Bacteroides fragilis NCTC 9343],3CLW_C Crystal structure of conserved exported protein from Bacteroides fragilis [Bacteroides fragilis NCTC 9343],3CLW_D Crystal structure of conserved exported protein from Bacteroides fragilis [Bacteroides fragilis NCTC 9343],3CLW_E Crystal structure of conserved exported protein from Bacteroides fragilis [Bacteroides fragilis NCTC 9343],3CLW_F Crystal structure of conserved exported protein from Bacteroides fragilis [Bacteroides fragilis NCTC 9343]
7O0E_A 5.77e-09 68 172 296 386
ChainA, GH30 family xylanase [Thermothelomyces thermophilus ATCC 42464],7O0E_G Chain G, GH30 family xylanase [Thermothelomyces thermophilus ATCC 42464]
7NCX_AAA 6.13e-09 68 172 303 393
ChainAAA, GH30 family xylanase [Thermothelomyces thermophilus ATCC 42464]
1NOF_A 2.37e-06 3 184 195 335
ChainA, xylanase [Dickeya chrysanthemi],2Y24_A Chain A, XYLANASE [Dickeya chrysanthemi]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
G2Q1N4 3.33e-08 68 172 320 410
GH30 family xylanase OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=Xyn30A PE=1 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
1.000051 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001666_00674.