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CAZyme Information: MGYG000004085_00889

You are here: Home > Sequence: MGYG000004085_00889

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; Monoglobales_A; UMGS1253; UMGS1253;
CAZyme ID MGYG000004085_00889
CAZy Family PL35
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1406 MGYG000004085_3|CGC3 155929.24 4.2637
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004085 2144710 MAG United Kingdom Europe
Gene Location Start: 91396;  End: 95616  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004085_00889.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL35 925 1098 1.9e-42 0.9664804469273743
CBM32 1288 1402 4.4e-20 0.8790322580645161

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07833 Cu_amine_oxidN1 6.75e-24 447 536 2 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 7.52e-15 399 476 16 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 4.46e-14 1282 1401 3 127
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
pfam07940 Hepar_II_III 0.002 940 1090 39 185
Heparinase II/III-like protein. This family features sequences that are similar to a region of the Flavobacterium heparinum proteins heparinase II and heparinase III. The former is known to degrade heparin and heparin sulphate, whereas the latter predominantly degrades heparin sulphate. Both are secreted into the periplasmic space upon induction with heparin.
cd00057 FA58C 0.003 1313 1384 46 125
Substituted updates: Jan 31, 2002

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUH30172.1 9.30e-148 575 1399 71 888
AZS17848.1 4.39e-145 289 1400 133 1273
ALS27107.1 3.75e-126 556 1402 677 1509
SDS98549.1 1.08e-120 577 1400 52 854
QEH43197.1 1.49e-116 574 1149 30 600

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5ZU6_A 4.07e-23 1300 1404 52 157
ACBM32 derived from alginate lyase B (AlyB-OU02) [Vibrio]
5ZU5_A 1.07e-20 1300 1404 52 157
Crystalstructure of a full length alginate lyase with CBM domain [Vibrio splendidus]
7D29_A 1.63e-14 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 7.11e-13 1300 1402 29 130
TruncatedAlyQ with CBM32 and alginate lyase domains [Persicobacter sp. CCB-QB2]
2JD9_A 3.93e-10 1300 1402 31 132
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
0.000245 0.999125 0.000162 0.000168 0.000155 0.000144

TMHMM  Annotations      download full data without filtering help

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