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CAZyme Information: MGYG000004128_00767

You are here: Home > Sequence: MGYG000004128_00767

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 UMGS1253 sp900550065
Lineage Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UMGS1253; UMGS1253; UMGS1253 sp900550065
CAZyme ID MGYG000004128_00767
CAZy Family PL35
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1406 MGYG000004128_21|CGC1 156373.26 4.6173
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004128 2239270 MAG United Kingdom Europe
Gene Location Start: 16186;  End: 20406  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004128_00767.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL35 926 1098 1.6e-41 0.9608938547486033
CBM32 1283 1402 3.9e-20 0.9354838709677419

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07833 Cu_amine_oxidN1 1.94e-26 446 536 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 4.71e-15 392 476 10 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.
pfam00754 F5_F8_type_C 5.11e-14 1282 1401 3 127
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
pfam16332 DUF4962 2.42e-07 573 853 133 417
Domain of unknown function (DUF4962). This family consists of uncharacterized proteins around 870 residues in length and is mainly found in various Bacteroides species. The function of this protein is unknown.
cd00057 FA58C 0.001 1283 1356 16 92
Substituted updates: Jan 31, 2002

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUH30172.1 2.37e-150 575 1399 71 888
AZS17848.1 1.72e-147 268 1400 108 1273
ALS27107.1 1.65e-127 556 1402 677 1509
SDS98549.1 2.31e-122 577 1400 52 854
QNK58643.1 8.74e-120 543 1400 759 1605

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5ZU6_A 3.44e-24 1305 1404 57 157
ACBM32 derived from alginate lyase B (AlyB-OU02) [Vibrio]
5ZU5_A 1.09e-21 1305 1404 57 157
Crystalstructure of a full length alginate lyase with CBM domain [Vibrio splendidus]
7D29_A 2.55e-15 1300 1402 29 130
CBM32of AlyQ [Persicobacter sp. CCB-QB2],7D2A_A CBM32 of AlyQ in complex with 4,5-unsaturated mannuronic acid [Persicobacter sp. CCB-QB2]
5XNR_A 1.28e-13 1300 1402 29 130
TruncatedAlyQ with CBM32 and alginate lyase domains [Persicobacter sp. CCB-QB2]
2JD9_A 1.32e-11 1277 1402 9 132
Structureof a pectin binding carbohydrate binding module determined in an orthorhombic crystal form. [Yersinia enterocolitica],2JDA_A Structure of a pectin binding carbohydrate binding module determined in an monoclinic crystal form. [Yersinia enterocolitica],2JDA_B Structure of a pectin binding carbohydrate binding module determined in an monoclinic crystal form. [Yersinia enterocolitica]

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
0.000721 0.516622 0.481912 0.000314 0.000240 0.000190

TMHMM  Annotations      download full data without filtering help

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