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CAZyme Information: MGYG000000574_02592

You are here: Home > Sequence: MGYG000000574_02592

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; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; ;
CAZyme ID MGYG000000574_02592
CAZy Family GH78
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
417 47685.66 5.187
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000574 5306470 MAG Madagascar Africa
Gene Location Start: 2788;  End: 4041  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.40

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH78 3 382 9.5e-86 0.746031746031746

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam17389 Bac_rhamnosid6H 3.34e-20 5 338 4 339
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.
COG3408 GDB1 1.18e-07 82 206 335 465
Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism].
pfam06202 GDE_C 2.34e-07 82 209 80 217
Amylo-alpha-1,6-glucosidase. This family includes human glycogen branching enzyme AGL. This enzyme contains a number of distinct catalytic activities. It has been shown for the yeast homolog GDB1 that mutations in this region disrupt the enzymes Amylo-alpha-1,6-glucosidase (EC:3.2.1.33).

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QRQ48848.1 1.66e-137 4 412 286 697
QUT45325.1 2.34e-137 4 412 286 697
QIK55686.1 1.94e-135 4 388 291 675
AXP80063.1 2.62e-135 4 401 279 674
QUT83668.1 3.10e-135 4 382 300 678

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3CIH_A 3.02e-127 4 401 301 697
Crystalstructure of a putative alpha-rhamnosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
4XHC_A 1.62e-28 9 338 211 541
ChainA, Alpha-L-rhamnosidase [Klebsiella oxytoca],4XHC_B Chain B, Alpha-L-rhamnosidase [Klebsiella oxytoca]
1V7V_A 3.60e-08 83 248 422 601
Crystalstructure of Vibrio proteolyticus chitobiose phosphorylase [Vibrio proteolyticus],1V7W_A Crystal structure of Vibrio proteolyticus chitobiose phosphorylase in complex with GlcNAc [Vibrio proteolyticus],1V7X_A Crystal structure of Vibrio proteolyticus chitobiose phosphorylase in complex with GlcNAc and sulfate [Vibrio proteolyticus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
T2KM26 5.78e-09 6 371 732 1102
Bifunctional sulfatase/alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22250 PE=1 SV=2
Q76IQ9 1.97e-07 83 248 422 601
N,N'-diacetylchitobiose phosphorylase OS=Vibrio proteolyticus OX=671 GN=chbP PE=1 SV=1
P9WF03 6.27e-07 7 377 472 853
Alpha-L-rhamnosidase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_34 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
1.000071 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000574_02592.