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CAZyme Information: MGYG000000495_01910

You are here: Home > Sequence: MGYG000000495_01910

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 HGM11501 sp900766735
Lineage Bacteria; Firmicutes_A; Clostridia; UMGS1883; HGM11501; HGM11501; HGM11501 sp900766735
CAZyme ID MGYG000000495_01910
CAZy Family GH26
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
651 72009.24 4.9945
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000495 2149207 MAG Fiji Oceania
Gene Location Start: 11503;  End: 13458  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000495_01910.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH26 359 487 2.2e-18 0.37623762376237624

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07833 Cu_amine_oxidN1 7.40e-28 46 136 3 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 5.52e-08 355 489 167 305
Beta-mannanase [Carbohydrate transport and metabolism].
pfam07833 Cu_amine_oxidN1 1.84e-06 106 134 1 29
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 4.42e-06 359 496 143 272
Glycosyl hydrolase family 26.
pfam07833 Cu_amine_oxidN1 0.003 41 74 60 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QSX05302.1 1.20e-140 1 651 9 666
AZN43604.1 8.54e-83 153 651 29 536
BBH22216.1 9.47e-83 220 651 103 540
QHT63759.1 2.53e-79 156 651 4 507
AMY96565.1 3.96e-79 220 651 24 461

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
0.000291 0.998944 0.000206 0.000176 0.000168 0.000159

TMHMM  Annotations      download full data without filtering help

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