Species | Parabacteroides sp900548175 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp900548175 | |||||||||||
CAZyme ID | MGYG000001878_01002 | |||||||||||
CAZy Family | GH33 | |||||||||||
CAZyme Description | Hercynine oxygenase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 42075; End: 44093 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH33 | 311 | 608 | 1.8e-27 | 0.827485380116959 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG1262 | YfmG | 2.73e-48 | 30 | 251 | 53 | 311 | Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones]. |
pfam03781 | FGE-sulfatase | 1.55e-46 | 30 | 250 | 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. |
cd15482 | Sialidase_non-viral | 1.29e-36 | 301 | 608 | 6 | 302 | 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 | 6.40e-25 | 320 | 608 | 1 | 260 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
TIGR02171 | Fb_sc_TIGR02171 | 7.12e-15 | 51 | 250 | 61 | 280 | Fibrobacter succinogenes paralogous family TIGR02171. This model describes a paralogous family of the rumen bacterium Fibrobacter succinogenes. Eleven members are found in Fibrobacter succinogenes S85, averaging over 900 amino acids in length. More than half are predicted lipoproteins. The function is unknown. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QNL36993.1 | 0.0 | 28 | 661 | 26 | 661 |
SCV08950.1 | 0.0 | 28 | 661 | 26 | 661 |
ALJ49526.1 | 0.0 | 28 | 661 | 26 | 661 |
QRQ56304.1 | 0.0 | 28 | 661 | 26 | 661 |
QGT74043.1 | 0.0 | 28 | 661 | 26 | 661 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5HHA_A | 1.66e-31 | 21 | 249 | 35 | 282 | Structureof PvdO from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],5HHA_B Structure of PvdO from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1] |
6MUJ_A | 9.48e-23 | 31 | 248 | 32 | 305 | Formylglycinegenerating enzyme bound to copper [Streptomyces coelicolor A3(2)],6MUJ_B Formylglycine generating enzyme bound to copper [Streptomyces coelicolor A3(2)],6MUJ_C Formylglycine generating enzyme bound to copper [Streptomyces coelicolor A3(2)],6MUJ_D Formylglycine generating enzyme bound to copper [Streptomyces coelicolor A3(2)],6MUJ_E Formylglycine generating enzyme bound to copper [Streptomyces coelicolor A3(2)] |
2Q17_A | 1.45e-22 | 31 | 248 | 59 | 332 | FormylglycineGenerating Enzyme from Streptomyces coelicolor [Streptomyces coelicolor A3(2)],2Q17_B Formylglycine Generating Enzyme from Streptomyces coelicolor [Streptomyces coelicolor A3(2)],2Q17_C Formylglycine Generating Enzyme from Streptomyces coelicolor [Streptomyces coelicolor A3(2)],2Q17_D Formylglycine Generating Enzyme from Streptomyces coelicolor [Streptomyces coelicolor A3(2)],2Q17_E Formylglycine Generating Enzyme from Streptomyces coelicolor [Streptomyces coelicolor A3(2)] |
5NXL_A | 3.79e-20 | 29 | 248 | 16 | 294 | Formylglycinegenerating enzyme from T. curvata in complex with Ag(I) [Thermomonospora curvata DSM 43183],5NYY_A Formylglycine generating enzyme from T. curvata in complex with Cd(II) [Thermomonospora curvata DSM 43183] |
6S07_A | 3.98e-20 | 21 | 248 | 13 | 298 | Structureof formylglycine-generating enzyme at 1.04 A in complex with copper and substrate reveals an acidic pocket for binding and acti-vation of molecular oxygen. [Thermomonospora curvata DSM 43183],6XTL_A Chain A, Formylglycine-generating enzyme [Thermomonospora curvata DSM 43183],6XTM_A Chain A, Formylglycine-generating enzyme [Thermomonospora curvata DSM 43183],6XTN_A Chain A, Formylglycine-generating enzyme [Thermomonospora curvata DSM 43183],6XTO_A Chain A, Formylglycine-generating enzyme [Thermomonospora curvata DSM 43183],6XTP_A Chain A, Formylglycine-generating enzyme [Thermomonospora curvata DSM 43183],6XTQ_A Chain A, Formylglycine-generating enzyme [Thermomonospora curvata DSM 43183],6XTR_A Chain A, Formylglycine-generating enzyme [Thermomonospora curvata DSM 43183],6XTS_A Chain A, Formylglycine-generating enzyme [Thermomonospora curvata DSM 43183] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9F3C7 | 4.77e-22 | 31 | 248 | 27 | 300 | Formylglycine-generating enzyme OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=SCO7548 PE=1 SV=1 |
Q7AJA5 | 6.69e-21 | 29 | 252 | 384 | 617 | Serine/threonine-protein kinase pkn1 OS=Chlamydia pneumoniae OX=83558 GN=pkn1 PE=3 SV=1 |
D1A7C3 | 2.18e-19 | 21 | 248 | 12 | 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 |
Q0P5L5 | 5.79e-19 | 26 | 248 | 87 | 364 | Formylglycine-generating enzyme OS=Bos taurus OX=9913 GN=SUMF1 PE=2 SV=1 |
Q8NBK3 | 5.79e-19 | 23 | 248 | 84 | 364 | Formylglycine-generating enzyme OS=Homo sapiens OX=9606 GN=SUMF1 PE=1 SV=3 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000972 | 0.998075 | 0.000366 | 0.000192 | 0.000204 | 0.000195 |
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