logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001898_01072

You are here: Home > Sequence: MGYG000001898_01072

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 Parabacteroides sp900552415
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp900552415
CAZyme ID MGYG000001898_01072
CAZy Family GH33
CAZyme Description Hercynine oxygenase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
659 MGYG000001898_29|CGC1 73745.8 6.0621
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001898 3107743 MAG Denmark Europe
Gene Location Start: 3446;  End: 5425  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001898_01072.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH33 307 644 2.2e-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 3.36e-45 25 245 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 2.55e-43 25 247 53 312
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones].
cd15482 Sialidase_non-viral 5.31e-36 302 644 11 321
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 9.86e-26 316 643 1 280
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
COG4692 COG4692 0.007 305 559 33 274
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
SCV08950.1 0.0 10 657 3 661
ALJ49526.1 0.0 10 657 3 661
QRQ56304.1 0.0 10 657 3 661
QGT74043.1 0.0 10 657 3 661
QNL36993.1 0.0 10 657 3 661

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5HHA_A 6.20e-32 25 244 42 282
Structureof PvdO from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],5HHA_B Structure of PvdO from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1]
6MUJ_A 6.69e-20 26 243 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 9.77e-20 26 243 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 5.47e-19 25 243 17 294
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 5.74e-19 25 243 21 298
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9F3C7 3.40e-19 26 243 27 300
Formylglycine-generating enzyme OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=SCO7548 PE=1 SV=1
Q0P5L5 1.01e-18 20 252 86 373
Formylglycine-generating enzyme OS=Bos taurus OX=9913 GN=SUMF1 PE=2 SV=1
Q7AJA5 1.01e-18 25 243 385 613
Serine/threonine-protein kinase pkn1 OS=Chlamydia pneumoniae OX=83558 GN=pkn1 PE=3 SV=1
D1A7C3 3.14e-18 25 243 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
Q822R1 1.26e-17 25 243 384 612
Serine/threonine-protein kinase pkn1 OS=Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC) OX=227941 GN=pkn1 PE=3 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
0.000363 0.998951 0.000182 0.000179 0.000154 0.000151

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001898_01072.