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CAZyme Information: MGYG000004439_00009

You are here: Home > Sequence: MGYG000004439_00009

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; ;
CAZyme ID MGYG000004439_00009
CAZy Family GH26
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
560 62596.54 4.4664
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004439 2174785 MAG Israel Asia
Gene Location Start: 9752;  End: 11434  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004439_00009.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH26 99 232 1.4e-17 0.429042904290429

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07833 Cu_amine_oxidN1 1.59e-38 467 559 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-12 434 496 30 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 6.70e-09 529 560 1 32
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 6.78e-07 128 250 162 291
Beta-mannanase [Carbohydrate transport and metabolism].
pfam02156 Glyco_hydro_26 5.72e-06 127 270 136 286
Glycosyl hydrolase family 26.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AUO18272.1 2.64e-94 21 432 183 619
AUO19576.1 4.92e-84 43 559 49 579
BAD39558.1 8.53e-52 63 559 86 586
AEI42662.1 6.71e-49 27 559 133 666
AFH64572.2 9.47e-49 27 559 136 669

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 3.77e-07 433 558 18 141
Protease inhibitor OS=Brevibacillus choshinensis OX=54911 PE=1 SV=1

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
0.000336 0.998840 0.000210 0.000210 0.000194 0.000173

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004439_00009.