logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002719_00596

You are here: Home > Sequence: MGYG000002719_00596

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; HGM11514; HGM11514; ;
CAZyme ID MGYG000002719_00596
CAZy Family GH141
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
834 MGYG000002719_26|CGC1 93261.28 4.3909
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002719 3080250 MAG Canada North America
Gene Location Start: 3145;  End: 5649  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002719_00596.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH141 30 308 3e-21 0.4648956356736243

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07833 Cu_amine_oxidN1 1.70e-25 720 809 1 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 1.85e-11 690 750 38 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.
pfam13229 Beta_helix 9.88e-11 342 546 1 156
Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.
pfam13229 Beta_helix 6.59e-07 325 413 53 135
Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.
pfam13229 Beta_helix 0.003 323 411 74 157
Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUH28384.1 3.96e-140 29 680 38 727
QNK56945.1 7.05e-85 20 681 28 733
AUP78440.1 1.03e-62 30 680 26 683
QIJ77206.1 4.51e-52 216 628 212 625
QUT84604.1 1.03e-51 124 678 138 719

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
0.007897 0.990762 0.000555 0.000249 0.000249 0.000266

TMHMM  Annotations      download full data without filtering help

start end
5 23