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CAZyme Information: MGYG000001902_01019

You are here: Home > Sequence: MGYG000001902_01019

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; UMGS1810; UMGS1810; UMGS1810;
CAZyme ID MGYG000001902_01019
CAZy Family GH26
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
569 62908.72 4.5229
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001902 1713632 MAG Denmark Europe
Gene Location Start: 9674;  End: 11383  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001902_01019.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH26 127 294 6.6e-18 0.46534653465346537

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07833 Cu_amine_oxidN1 2.74e-40 473 565 1 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.
pfam07833 Cu_amine_oxidN1 1.26e-13 447 502 28 92
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 2.27e-10 535 568 1 34
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.
pfam02156 Glyco_hydro_26 8.75e-08 127 269 135 284
Glycosyl hydrolase family 26.
PRK14696 tynA 1.78e-06 478 531 1 54
primary-amine oxidase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AUO18272.1 2.71e-97 22 438 183 624
AUO19576.1 7.10e-82 44 566 49 580
BAD39558.1 1.59e-55 83 566 117 587
ALS21301.1 3.96e-46 28 566 133 667
AEI42662.1 2.64e-45 28 566 133 667

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P43131 2.18e-08 454 564 31 141
Protease inhibitor OS=Brevibacillus choshinensis OX=54911 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
0.000494 0.415712 0.583269 0.000184 0.000169 0.000157

TMHMM  Annotations      download full data without filtering help

start end
5 27