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CAZyme Information: MGYG000001253_00327

You are here: Home > Sequence: MGYG000001253_00327

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 Paramuribaculum sp001689535
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Paramuribaculum; Paramuribaculum sp001689535
CAZyme ID MGYG000001253_00327
CAZy Family GH33
CAZyme Description Hercynine oxygenase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
663 MGYG000001253_2|CGC4 72233 6.5457
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001253 2271514 MAG Austria Europe
Gene Location Start: 169836;  End: 171827  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001253_00327.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH33 309 646 1.2e-24 0.8801169590643275

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam03781 FGE-sulfatase 1.08e-48 24 249 1 258
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 3.51e-46 22 250 47 311
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones].
cd15482 Sialidase_non-viral 5.65e-37 299 646 6 321
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 4.29e-21 318 645 1 280
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
COG4692 COG4692 5.17e-05 278 559 7 272
Predicted neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QQR10361.1 3.55e-296 27 659 20 653
ASB36855.1 4.25e-296 27 659 25 658
ANU62655.1 4.25e-296 27 659 25 658
SCV08950.1 1.88e-292 28 661 28 663
ALJ49526.1 1.88e-292 28 661 28 663

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5HHA_A 1.18e-25 26 248 40 282
Structureof PvdO from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],5HHA_B Structure of PvdO from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1]
2AFT_X 6.49e-21 27 247 5 279
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 1.19e-20 27 247 5 279
ChainX, Sulfatase modifying factor 1 [Homo sapiens]
2AII_X 1.19e-20 27 247 5 279
wild-typeFormylglycine generating enzyme reacted with iodoacetamide [Homo sapiens]
1Y1E_X 1.80e-20 27 247 18 292
humanformylglycine generating enzyme [Homo sapiens],1Y1H_X human formylglycine generating enzyme, oxidised Cys refined as hydroperoxide [Homo sapiens],1Y1I_X hyuman formylglycine generating enzyme, reduced form [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8R0F3 1.61e-20 27 247 88 362
Formylglycine-generating enzyme OS=Mus musculus OX=10090 GN=Sumf1 PE=1 SV=2
Q0P5L5 9.68e-20 27 247 90 364
Formylglycine-generating enzyme OS=Bos taurus OX=9913 GN=SUMF1 PE=2 SV=1
Q8NBK3 2.34e-19 27 247 90 364
Formylglycine-generating enzyme OS=Homo sapiens OX=9606 GN=SUMF1 PE=1 SV=3
D1A7C3 1.29e-18 28 247 20 297
Formylglycine-generating enzyme OS=Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9) OX=471852 GN=Tcur_4811 PE=1 SV=1
Q9F3C7 1.66e-17 29 247 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
0.000271 0.999004 0.000181 0.000192 0.000176 0.000154

TMHMM  Annotations      download full data without filtering help

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