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CAZyme Information: MGYG000002414_03139

You are here: Home > Sequence: MGYG000002414_03139

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 Paenibacillus odorifer
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus odorifer
CAZyme ID MGYG000002414_03139
CAZy Family GH136
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
2265 MGYG000002414_1|CGC67 243292.03 4.6435
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002414 6802552 Isolate South Korea Asia
Gene Location Start: 3573088;  End: 3579885  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002414_03139.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH136 1028 1609 4e-92 0.9918533604887984

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07833 Cu_amine_oxidN1 1.89e-26 2178 2263 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 1.36e-15 2144 2208 29 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.
pfam09479 Flg_new 2.51e-13 1612 1677 1 65
Listeria-Bacteroides repeat domain (List_Bact_rpt). This model describes a conserved core region of about 43 residues, which occurs in at least two families of tandem repeats. These include 78-residue repeats which occur from 2 to 15 times in some proteins of Bacteroides forsythus ATCC 43037, and 70-residue repeats found in families of internalins of Listeria species. Single copies are found in proteins of Fibrobacter succinogenes, Geobacter sulfurreducens, and a few other bacteria.
pfam05345 He_PIG 4.30e-08 1867 1950 1 95
Putative Ig domain. This alignment represents the conserved core region of ~90 residue repeat found in several haemagglutinins and other cell surface proteins. Sequence similarities to (pfam02494) and (pfam00801) suggest an Ig-like fold (personal obs:C. Yeats). So this family may be similar in function to the (pfam02639) and (pfam02638) domains. This domain is also found in the WisP family of proteins of Tropheryma whipplei.
NF033189 internalin_A 1.29e-06 1590 1692 612 716
class 1 internalin InlA. Internalins, as found in the intracellular human pathogen Listeria monocytogenes, are paralogous surface or secreted proteins with an N-terminal signal peptide, leucine-rich repeats, and usually a C-terminal LPXTG processing and cell surface anchoring site. See PMID:17764999 for a general discussion of internalins. Members of this family are internalin A (InlA), a class 1 (LPXTG-type) internalin.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AWV33927.1 0.0 1 2265 1 2265
AIQ74599.1 0.0 1 2265 1 2265
AIQ24130.1 0.0 1 2265 1 2257
AIQ35957.1 0.0 1 2265 1 2258
AZS16171.1 0.0 1 2265 1 2280

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4OGZ_A 3.25e-06 1853 1949 3 92
Crystalstructure of a putative alpha-galactosidase/melibiase (BF4189) from Bacteroides fragilis NCTC 9343 at 2.00 A resolution [Bacteroides fragilis NCTC 9343],4OGZ_B Crystal structure of a putative alpha-galactosidase/melibiase (BF4189) from Bacteroides fragilis NCTC 9343 at 2.00 A resolution [Bacteroides fragilis NCTC 9343]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P0DJ97 1.06e-13 1610 1678 661 729
Putative Gly-rich membrane protein Bcell_0380 OS=Evansella cellulosilytica (strain ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4) OX=649639 GN=Bcell_0380 PE=4 SV=1
P0DJ98 4.38e-13 1610 1678 81 149
Putative membrane protein Bcell_0381 OS=Evansella cellulosilytica (strain ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4) OX=649639 GN=Bcell_0381 PE=4 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
0.000291 0.998955 0.000184 0.000208 0.000175 0.000148

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002414_03139.