logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004223_01596

You are here: Home > Sequence: MGYG000004223_01596

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 UMGS1883 sp900763305
Lineage Bacteria; Firmicutes_A; Clostridia; UMGS1883; UMGS1883; UMGS1883; UMGS1883 sp900763305
CAZyme ID MGYG000004223_01596
CAZy Family GH26
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
656 MGYG000004223_13|CGC2 72078.88 5.1749
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004223 2575981 MAG United Kingdom Europe
Gene Location Start: 47458;  End: 49428  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004223_01596.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH26 342 490 6.3e-19 0.44554455445544555

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07833 Cu_amine_oxidN1 3.53e-28 44 132 1 89
Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.
pfam07833 Cu_amine_oxidN1 6.10e-08 19 74 41 93
Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.
COG4124 ManB2 1.25e-06 271 513 77 336
Beta-mannanase [Carbohydrate transport and metabolism].
PRK14696 tynA 0.002 49 112 1 64
primary-amine oxidase.
pfam02156 Glyco_hydro_26 0.003 363 449 143 232
Glycosyl hydrolase family 26.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QSX05302.1 7.53e-179 19 655 26 665
AZN43604.1 6.99e-102 157 649 31 530
QNK58256.1 2.44e-96 152 656 31 538
QHT63759.1 1.38e-95 158 656 4 507
AMY96565.1 3.04e-94 199 656 1 461

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000228 0.999103 0.000164 0.000168 0.000160 0.000146

TMHMM  Annotations      download full data without filtering help

start end
5 27