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CAZyme Information: MGYG000001804_01857

You are here: Home > Sequence: MGYG000001804_01857

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; UBA932; CAG-831;
CAZyme ID MGYG000001804_01857
CAZy Family GH53
CAZyme Description Arabinogalactan endo-beta-1,4-galactanase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
368 MGYG000001804_96|CGC1 41211.86 4.1306
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001804 2176227 MAG Denmark Europe
Gene Location Start: 1427;  End: 2533  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.89

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH53 45 366 3.6e-98 0.9941520467836257

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07745 Glyco_hydro_53 4.67e-98 44 366 1 333
Glycosyl hydrolase family 53. This domain belongs to family 53 of the glycosyl hydrolase classification. These enzymes are enzymes are endo-1,4- beta-galactanases (EC:3.2.1.89). The structure of this domain is known and has a TIM barrel fold.
COG3867 GanB 2.74e-85 43 367 39 392
Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism].
smart00922 MR_MLE 0.007 71 121 7 53
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain. Mandelate racemase (MR) and muconate lactonizing enzyme (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures.. This entry represents the C-terminal region of these proteins.
pfam13378 MR_MLE_C 0.008 77 168 1 88
Enolase C-terminal domain-like. This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N pfam02746 domain. EC:4.2.1.40.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
SCD19010.1 3.85e-125 39 367 35 344
QIK60890.1 3.98e-125 12 368 8 346
QIK55473.1 1.79e-123 43 367 40 345
APU98489.1 1.14e-120 43 367 35 340
QMV66380.1 1.31e-119 43 367 35 340

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6GPA_A 6.78e-94 40 367 4 314
Beta-1,4-galactanasefrom Bacteroides thetaiotaomicron with galactose [Bacteroides thetaiotaomicron VPI-5482],6GPA_B Beta-1,4-galactanase from Bacteroides thetaiotaomicron with galactose [Bacteroides thetaiotaomicron VPI-5482]
6GP5_A 2.28e-93 40 367 40 350
Beta-1,4-galactanasefrom Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],6GP5_B Beta-1,4-galactanase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
1HJS_A 5.27e-38 45 367 5 330
Structureof two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_B Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_C Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_D Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_A Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_B Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_C Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_D Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus]
7OSK_A 8.65e-38 43 300 50 301
ChainA, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230],7OSK_B Chain B, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230]
1HJQ_A 3.88e-37 45 366 5 329
Structureof two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Humicola insolens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P48843 3.10e-51 40 334 3 315
Uncharacterized protein in bgaB 5'region (Fragment) OS=Niallia circulans OX=1397 PE=3 SV=1
P83692 2.88e-37 45 367 5 330
Arabinogalactan endo-beta-1,4-galactanase OS=Thermothelomyces thermophilus OX=78579 PE=1 SV=1
P83691 2.12e-36 45 366 5 329
Arabinogalactan endo-beta-1,4-galactanase OS=Humicola insolens OX=34413 PE=1 SV=1
Q0CTQ7 8.21e-36 45 336 19 317
Probable arabinogalactan endo-beta-1,4-galactanase A OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=galA PE=3 SV=1
Q65CX5 4.47e-35 43 256 49 265
Endo-beta-1,4-galactanase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=ganB PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000000 1.000064 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001804_01857.