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CAZyme Information: MGYG000001735_02789

You are here: Home > Sequence: MGYG000001735_02789

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; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides;
CAZyme ID MGYG000001735_02789
CAZy Family GH33
CAZyme Description Hercynine oxygenase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
679 MGYG000001735_36|CGC1 76553.33 6.7569
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001735 5309957 MAG Sweden Europe
Gene Location Start: 29972;  End: 32011  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001735_02789.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH33 327 624 1e-23 0.827485380116959

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam03781 FGE-sulfatase 1.28e-51 45 265 5 258
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 2.29e-49 45 267 53 312
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones].
cd15482 Sialidase_non-viral 4.81e-32 316 664 5 321
Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
pfam13088 BNR_2 6.61e-23 336 624 1 260
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
SCV08950.1 0.0 18 679 1 663
ALJ49526.1 0.0 18 679 1 663
QRQ56304.1 0.0 18 679 1 663
QNL36993.1 0.0 18 679 1 663
QGT74043.1 0.0 18 679 1 663

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5HHA_A 1.46e-26 45 264 42 282
Structureof PvdO from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],5HHA_B Structure of PvdO from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1]
2AFT_X 2.68e-26 45 270 6 286
ChainX, Sulfatase modifying factor 1 [Homo sapiens],2AIJ_X Chain X, Sulfatase modifying factor 1 [Homo sapiens],2AIK_X Chain X, Sulfatase modifying factor 1 [Homo sapiens],2HI8_X Chain X, Sulfatase-modifying factor 1 [Homo sapiens],2HIB_X Chain X, Sulfatase-modifying factor 1 [Homo sapiens]
2AFY_X 2.68e-26 45 270 6 286
ChainX, Sulfatase modifying factor 1 [Homo sapiens]
2AII_X 4.94e-26 45 270 6 286
wild-typeFormylglycine generating enzyme reacted with iodoacetamide [Homo sapiens]
1Y1G_X 5.97e-26 45 270 19 299
Humanformylglycine generating enzyme, double sulfonic acid form [Homo sapiens],1Z70_X 1.15A resolution structure of the formylglycine generating enzyme FGE [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q0P5L5 2.87e-25 39 270 85 371
Formylglycine-generating enzyme OS=Bos taurus OX=9913 GN=SUMF1 PE=2 SV=1
Q8R0F3 6.83e-25 35 270 79 369
Formylglycine-generating enzyme OS=Mus musculus OX=10090 GN=Sumf1 PE=1 SV=2
Q7AJA5 1.06e-24 36 263 375 613
Serine/threonine-protein kinase pkn1 OS=Chlamydia pneumoniae OX=83558 GN=pkn1 PE=3 SV=1
Q8NBK3 1.28e-24 45 270 91 371
Formylglycine-generating enzyme OS=Homo sapiens OX=9606 GN=SUMF1 PE=1 SV=3
Q9F3C7 5.89e-23 46 263 27 300
Formylglycine-generating enzyme OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=SCO7548 PE=1 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
0.174576 0.821875 0.002743 0.000265 0.000239 0.000282

TMHMM  Annotations      download full data without filtering help

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