logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000069_01889

You are here: Home > Sequence: MGYG000000069_01889

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 Clostridium_A leptum
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Clostridium_A; Clostridium_A leptum
CAZyme ID MGYG000000069_01889
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
680 MGYG000000069_5|CGC1 77805.82 4.9267
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000069 3099132 Isolate United Kingdom Europe
Gene Location Start: 6871;  End: 8913  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000069_01889.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH29 24 365 3.6e-62 0.8901734104046243

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3669 AfuC 5.54e-50 30 498 10 430
Alpha-L-fucosidase [Carbohydrate transport and metabolism].
pfam01120 Alpha_L_fucos 7.56e-28 48 365 53 329
Alpha-L-fucosidase.
smart00812 Alpha_L_fucos 1.75e-24 70 360 77 326
Alpha-L-fucosidase. O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in 'clans'. Family 29 encompasses alpha-L-fucosidases, which is a lysosomal enzyme responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Deficiency of alpha-L-fucosidase results in the lysosomal storage disease fucosidosis.
pfam07691 PA14 7.41e-16 584 671 46 137
PA14 domain. This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dictyostelium prespore-cell-inducing factor Psi and in fibrocystin, the mammalian protein whose mutation leads to polycystic kidney and hepatic disease. The crystal structure of PA shows that this domain (named PA14 after its location in the PA20 pro-peptide) has a beta-barrel structure. The PA14 domain sequence suggests a binding function, rather than a catalytic role. The PA14 domain distribution is compatible with carbohydrate binding.
smart00758 PA14 1.48e-14 577 671 37 133
domain in bacterial beta-glucosidases other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
SDS54218.1 1.01e-111 5 501 27 508
AFD07421.1 1.26e-110 15 505 28 501
AFL85744.1 4.63e-109 4 498 25 505
QNE41964.1 3.16e-107 15 499 77 544
QEC54436.1 3.45e-106 11 505 36 513

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4ZRX_A 9.34e-88 11 506 12 466
Crystalstructure of a putative alpha-L-fucosidase (BACOVA_04357) from Bacteroides ovatus ATCC 8483 at 1.59 A resolution [Bacteroides ovatus ATCC 8483]
3EYP_A 1.71e-73 31 506 10 462
Crystalstructure of putative alpha-L-fucosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron],3EYP_B Crystal structure of putative alpha-L-fucosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron],4OUE_A Crystal structure of an a-L-Fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with IPTG [Bacteroides thetaiotaomicron VPI-5482],4OUE_B Crystal structure of an a-L-Fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with IPTG [Bacteroides thetaiotaomicron VPI-5482],4OZO_A Crystal structure of an a-L-fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with oNPTG [Bacteroides thetaiotaomicron VPI-5482],4OZO_B Crystal structure of an a-L-fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with oNPTG [Bacteroides thetaiotaomicron VPI-5482]
5K9H_A 8.89e-68 31 503 39 468
Crystalstructure of a glycoside hydrolase 29 family member from an unknown rumen bacterium [unidentified]
6ORG_A 1.84e-66 31 500 11 450
Crystalstructure of SpGH29 [Streptococcus pneumoniae TIGR4],6ORG_B Crystal structure of SpGH29 [Streptococcus pneumoniae TIGR4]
6OR4_A 2.54e-65 31 500 11 450
Crystalstructure of SpGH29 [Streptococcus pneumoniae TIGR4],6OR4_B Crystal structure of SpGH29 [Streptococcus pneumoniae TIGR4],6ORH_A Crystal structure of SpGH29 [Streptococcus pneumoniae TIGR4],6ORH_B Crystal structure of SpGH29 [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q7XUR3 1.25e-69 31 498 40 476
Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2
Q8GW72 5.03e-69 31 498 38 477
Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2
P10901 7.69e-07 75 184 106 223
Alpha-L-fucosidase OS=Dictyostelium discoideum OX=44689 GN=alfA PE=3 SV=1
P49713 9.70e-06 40 367 68 345
Putative alpha-L-fucosidase OS=Caenorhabditis elegans OX=6239 GN=W03G11.3 PE=3 SV=2

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
1.000079 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000069_01889.