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CAZyme Information: MGYG000003424_01920

You are here: Home > Sequence: MGYG000003424_01920

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 SFTJ01 sp004557385
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; SFTJ01; SFTJ01 sp004557385
CAZyme ID MGYG000003424_01920
CAZy Family GH33
CAZyme Description Hercynine oxygenase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
659 MGYG000003424_160|CGC1 73150.12 6.2792
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003424 2699357 MAG Fiji Oceania
Gene Location Start: 2379;  End: 4358  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003424_01920.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH33 303 601 5.1e-22 0.8245614035087719

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam03781 FGE-sulfatase 6.30e-52 22 246 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 1.06e-46 24 249 51 313
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones].
cd15482 Sialidase_non-viral 8.68e-31 299 643 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 2.02e-21 313 642 1 280
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
pfam15902 Sortilin-Vps10 1.39e-04 443 607 2 119
Sortilin, neurotensin receptor 3,. Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNL36993.1 2.65e-303 10 657 9 662
QGT74043.1 5.34e-303 26 657 28 662
SCV08950.1 6.18e-302 10 657 9 662
ALJ49526.1 6.18e-302 10 657 9 662
QRQ56304.1 6.18e-302 10 657 9 662

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5HHA_A 1.37e-30 24 245 40 282
Structureof PvdO from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],5HHA_B Structure of PvdO from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1]
6MUJ_A 9.80e-19 29 244 34 305
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 1.40e-18 29 244 61 332
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 1.47e-17 92 249 129 299
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 1.53e-17 92 249 133 303
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
Q7AJA5 2.29e-24 25 244 384 613
Serine/threonine-protein kinase pkn1 OS=Chlamydia pneumoniae OX=83558 GN=pkn1 PE=3 SV=1
Q822R1 9.45e-24 25 244 383 612
Serine/threonine-protein kinase pkn1 OS=Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC) OX=227941 GN=pkn1 PE=3 SV=1
A0A0H3MBJ2 2.03e-21 25 244 379 608
Serine/threonine-protein kinase Pkn1 OS=Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B) OX=471472 GN=pkn1 PE=1 SV=1
P0DPS7 2.03e-21 25 244 379 608
Serine/threonine-protein kinase Pkn1 OS=Chlamydia trachomatis (strain D/UW-3/Cx) OX=272561 GN=pkn1 PE=3 SV=1
Q9PKP3 2.69e-21 25 244 379 608
Serine/threonine-protein kinase pkn1 OS=Chlamydia muridarum (strain MoPn / Nigg) OX=243161 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
0.000517 0.998471 0.000273 0.000247 0.000242 0.000225

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003424_01920.