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CAZyme Information: MGYG000000360_00164

You are here: Home > Sequence: MGYG000000360_00164

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 UBA1829 sp900548385
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; UBA1829; UBA1829 sp900548385
CAZyme ID MGYG000000360_00164
CAZy Family GH39
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1058 117851.19 9.6806
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000360 4492877 MAG Sweden Europe
Gene Location Start: 209273;  End: 212449  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000360_00164.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH39 412 698 4.4e-17 0.6983758700696056

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam03781 FGE-sulfatase 1.17e-09 33 205 20 193
Sulfatase-modifying factor enzyme 1. This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.
COG1262 YfmG 4.51e-04 49 123 87 155
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones].
pfam00150 Cellulase 8.94e-04 459 585 100 242
Cellulase (glycosyl hydrolase family 5).

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AVM45195.1 2.44e-317 15 1056 17 1064
AVM44950.1 2.16e-17 464 786 414 717
AVM46768.1 6.16e-15 324 911 236 821
ABQ89504.1 8.16e-11 449 664 134 359
ABS02551.1 5.48e-10 387 655 89 393

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
0.000670 0.998436 0.000244 0.000217 0.000211 0.000190

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000360_00164.