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CAZyme Information: MGYG000002132_01098

You are here: Home > Sequence: MGYG000002132_01098

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 Monoglobus sp900542675
Lineage Bacteria; Firmicutes_A; Clostridia; Monoglobales; Monoglobaceae; Monoglobus; Monoglobus sp900542675
CAZyme ID MGYG000002132_01098
CAZy Family GH26
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
645 MGYG000002132_37|CGC1 71289.21 4.6573
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002132 1988610 MAG United States North America
Gene Location Start: 3012;  End: 4949  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002132_01098.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH26 223 379 6e-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 1.01e-32 549 643 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 1.32e-12 511 579 28 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 3.54e-10 613 645 1 33
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 8.62e-04 236 311 179 256
Beta-mannanase [Carbohydrate transport and metabolism].
pfam14344 DUF4397 0.006 475 566 11 110
Domain of unknown function (DUF4397). This presumed domain is functionally uncharacterized. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 120 amino acids in length.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AMJ39775.1 7.85e-71 2 538 7 545
BAD39558.1 1.15e-63 75 643 18 586
AUO19576.1 1.38e-63 126 643 47 579
SMB96926.1 6.44e-48 110 643 112 661
QGP91309.1 3.57e-47 79 645 60 651

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2DDX_A 8.24e-06 182 312 56 185
Crystalstructure of beta-1,3-xylanase from Vibrio sp. AX-4 [Vibrio sp. AX-4],3VPL_A Crystal structure of a 2-fluoroxylotriosyl complex of the Vibrio sp. AX-4 Beta-1,3-xylanase [Vibrio sp.]

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
0.000379 0.997650 0.001380 0.000188 0.000191 0.000179

TMHMM  Annotations      download full data without filtering help

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