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CAZyme Information: MGYG000003574_01635

You are here: Home > Sequence: MGYG000003574_01635

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 CAG-110 sp900770015
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-110; CAG-110 sp900770015
CAZyme ID MGYG000003574_01635
CAZy Family CBM67
CAZyme Description Hydroxyacylglutathione hydrolase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1132 128325.42 4.8689
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003574 3049750 MAG Fiji Oceania
Gene Location Start: 13655;  End: 17053  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003574_01635.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH78 575 1103 3.3e-141 0.9920634920634921
CBM67 397 520 9.9e-17 0.6477272727272727

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17389 Bac_rhamnosid6H 3.73e-100 678 1043 4 340
Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.
cd07712 MBLAC2-like_MBL-fold 8.74e-34 39 200 10 182
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain. Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.
pfam08531 Bac_rhamnosid_N 3.97e-30 407 563 1 169
Alpha-L-rhamnosidase N-terminal domain. This family consists of bacterial rhamnosidase A and B enzymes. This domain is probably involved in substrate recognition.
cd06262 metallo-hydrolase-like_MBL-fold 3.08e-25 34 163 6 148
mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.
pfam05592 Bac_rhamnosid 1.04e-22 575 671 2 102
Bacterial alpha-L-rhamnosidase concanavalin-like domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ATU64247.1 9.26e-317 258 1118 12 874
ARN19579.1 9.45e-317 265 1118 2 856
APO28640.1 1.02e-216 280 1046 22 804
APO28678.1 2.03e-215 280 1046 44 826
BBI36516.1 2.04e-192 265 1106 14 897

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3W5M_A 1.61e-113 265 1102 4 992
CrystalStructure of Streptomyces avermitilis alpha-L-rhamnosidase [Streptomyces avermitilis MA-4680 = NBRC 14893],3W5N_A Crystal Structure of Streptomyces avermitilis alpha-L-rhamnosidase complexed with L-rhamnose [Streptomyces avermitilis MA-4680 = NBRC 14893]
6I60_A 5.02e-109 277 1129 42 925
Structureof alpha-L-rhamnosidase from Dictyoglumus thermophilum [Dictyoglomus thermophilum H-6-12],6I60_B Structure of alpha-L-rhamnosidase from Dictyoglumus thermophilum [Dictyoglomus thermophilum H-6-12]
6GSZ_A 2.66e-93 265 1085 2 816
Crystalstructure of native alfa-L-rhamnosidase from Aspergillus terreus [Aspergillus terreus]
2ZO4_A 2.95e-09 37 200 21 233
Crystalstructure of metallo-beta-lactamase family protein TTHA1429 from Thermus thermophilus HB8 [Thermus thermophilus HB8]
2XF4_A 3.76e-09 37 162 12 151
Crystalstructure of Salmonella enterica serovar typhimurium YcbL [Salmonella enterica]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q82PP4 6.83e-113 265 1102 4 992
Alpha-L-rhamnosidase OS=Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) OX=227882 GN=SAVERM_828 PE=1 SV=1
T2KNB2 1.83e-107 276 1103 45 877
Alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22090 PE=1 SV=2
P9WF03 1.25e-100 277 1100 42 874
Alpha-L-rhamnosidase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_34 PE=1 SV=1
T2KPL4 6.64e-68 275 1094 40 892
Alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22170 PE=2 SV=1
Q5XD24 2.86e-08 36 166 32 178
Probable metallo-hydrolase M6_Spy0554 OS=Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394) OX=286636 GN=M6_Spy0554 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
1.000062 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003574_01635.