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Conserved domains on  [gi|2793106767|ref|WP_371917662|]
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MULTISPECIES: formylglycine-generating enzyme family protein [unclassified Pseudomonas]

Protein Classification

formylglycine-generating enzyme family protein( domain architecture ID 11441389)

formylglycine-generating enzyme family protein similar to human sulfatase-modifying factor 1 (SUMF1), which oxidizes a cysteine residue in the substrate sulfatase, to an active site 3-oxoalanine residue, also called C(alpha)-formylglycine

CATH:  3.90.1580.10
PubMed:  30824597|27862795|18625336
SCOP:  4000450

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YfmG COG1262
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain ...
 113-353 2.34e-30

Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440874 [Multi-domain]  Cd Length: 238  Bit Score: 118.95  E-value: 2.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793106767 113 YFIGKYEVTARQYAEVMAQAQSLASGEPAPacealqaevPQGMAGRLPKVKLSRFEAERfsavYSAWLTKYHkdllpvsg 192
Cdd:COG1262    46 FYIDKYEVTNAEYRAFVGWTLADGRNNPLY---------SDFGGPDHPVVHVSWYDAQA----YCRWLGKKT-------- 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793106767 193 rgtsaeegGLGFvRLPTEVEWEFAARGGqavsrqelEGRLFPrrlegsEGDGPLADWAVFNqvagGTGQAARLMPIGTKL 272
Cdd:COG1262   105 --------GKGY-RLPTEAEWEYAARGG--------DGRPYP------WGDDLPPELANYA----GNDGRGSTAPVGSFP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793106767 273 PNPIGLFDVIGNAAEMVQESFQLVHAGRRQ-GAYG-----GFVVKGGNYLEGEGTLFTGMRREYPlfaadgTEQSNETTG 346
Cdd:COG1262   158 PNPFGLYDMAGNVWEWTADWYDPPYPGAPAdGPVGpenggQRVLRGGSWATPPDHLRSAYRNFFP------PDARWQFVG 231


                  ....*..
gi 2793106767 347 FRVAIGA 353
Cdd:COG1262   232 FRLARDL 238
 
Name Accession Description Interval E-value
YfmG COG1262
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain ...
 113-353 2.34e-30

Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440874 [Multi-domain]  Cd Length: 238  Bit Score: 118.95  E-value: 2.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793106767 113 YFIGKYEVTARQYAEVMAQAQSLASGEPAPacealqaevPQGMAGRLPKVKLSRFEAERfsavYSAWLTKYHkdllpvsg 192
Cdd:COG1262    46 FYIDKYEVTNAEYRAFVGWTLADGRNNPLY---------SDFGGPDHPVVHVSWYDAQA----YCRWLGKKT-------- 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793106767 193 rgtsaeegGLGFvRLPTEVEWEFAARGGqavsrqelEGRLFPrrlegsEGDGPLADWAVFNqvagGTGQAARLMPIGTKL 272
Cdd:COG1262   105 --------GKGY-RLPTEAEWEYAARGG--------DGRPYP------WGDDLPPELANYA----GNDGRGSTAPVGSFP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793106767 273 PNPIGLFDVIGNAAEMVQESFQLVHAGRRQ-GAYG-----GFVVKGGNYLEGEGTLFTGMRREYPlfaadgTEQSNETTG 346
Cdd:COG1262   158 PNPFGLYDMAGNVWEWTADWYDPPYPGAPAdGPVGpenggQRVLRGGSWATPPDHLRSAYRNFFP------PDARWQFVG 231


                  ....*..
gi 2793106767 347 FRVAIGA 353
Cdd:COG1262   232 FRLARDL 238
FGE-sulfatase pfam03781
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
 80-351 1.32e-23

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.


Pssm-ID: 397722 [Multi-domain]  Cd Length: 259  Bit Score: 100.26  E-value: 1.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793106767  80 GQFTLKDLPKDWGKTITPLMPKTdsktpLKPmlYFIGKYEVTARQYAEVMAQ--------AQSLASGEPAPACEALQAEV 151
Cdd:pfam03781  11 GSFEMGSAERTGNDNEAPAHDVT-----VRP--FAIDKYPVTNAQYAAFVEAtgyttevyPQWWAEVEGANWRHPSGGLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793106767 152 PQGMAGRLPKVKLSRFEAErfsaVYSAWLtkyhkdllpvsGRGTsaeeggLGFVRLPTEVEWEFAARGGQAvsrqeleGR 231
Cdd:pfam03781  84 DIDDGADHPVTGVSWYDAV----AYARWL-----------GKRT------GNGYRLPTEAEWEYAARGGSK-------GR 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793106767 232 LFPRRLEGSEGDGPLADWAVFNQVAGGTGQAARLMPIGTKLPNPIGLFDVIGNAAEMVQESFQLVHAGRRQGAYGGF--- 308
Cdd:pfam03781 136 RYPWGDELYPAGNIWQGADFPNEHAGADSFNGRTSPVGSFPPNALGLYDMAGNVWEWTSDWYKPHYSFAPYDELSRDnfg 215

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2793106767 309 ----VVKGGNYLEGEGTLFtgMRREYPL-FAADGTEQSNetTGFRVAI 351
Cdd:pfam03781 216 ggyrVVRGGSWACSVYPSR--LRPAFRGnCQTPGTRADD--VGFRLVR 259
egtB_TIGR03440 TIGR03440
ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of ...
 206-245 5.01e-03

ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of the ergothioneine biosynthesis, as found in numerous Actinobacteria. Characterized homologs to this family include a formylglycine-generating enzyme that serves as a maturase for an aerobic sulfatase (cf. the radical SAM enzymes that serve as anaerobic sulfatase maturases). [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 274581 [Multi-domain]  Cd Length: 406  Bit Score: 39.62  E-value: 5.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2793106767 206 RLPTEVEWEFAARGGQAVSRQELEGRLFPRRLEGSEGDGP 245
Cdd:TIGR03440 291 RLPTEAEWEKAARWGDAPPNFAEANLGAPVGAYPAGAQGL 330
 
Name Accession Description Interval E-value
YfmG COG1262
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain ...
 113-353 2.34e-30

Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440874 [Multi-domain]  Cd Length: 238  Bit Score: 118.95  E-value: 2.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793106767 113 YFIGKYEVTARQYAEVMAQAQSLASGEPAPacealqaevPQGMAGRLPKVKLSRFEAERfsavYSAWLTKYHkdllpvsg 192
Cdd:COG1262    46 FYIDKYEVTNAEYRAFVGWTLADGRNNPLY---------SDFGGPDHPVVHVSWYDAQA----YCRWLGKKT-------- 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793106767 193 rgtsaeegGLGFvRLPTEVEWEFAARGGqavsrqelEGRLFPrrlegsEGDGPLADWAVFNqvagGTGQAARLMPIGTKL 272
Cdd:COG1262   105 --------GKGY-RLPTEAEWEYAARGG--------DGRPYP------WGDDLPPELANYA----GNDGRGSTAPVGSFP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793106767 273 PNPIGLFDVIGNAAEMVQESFQLVHAGRRQ-GAYG-----GFVVKGGNYLEGEGTLFTGMRREYPlfaadgTEQSNETTG 346
Cdd:COG1262   158 PNPFGLYDMAGNVWEWTADWYDPPYPGAPAdGPVGpenggQRVLRGGSWATPPDHLRSAYRNFFP------PDARWQFVG 231


                  ....*..
gi 2793106767 347 FRVAIGA 353
Cdd:COG1262   232 FRLARDL 238
FGE-sulfatase pfam03781
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
 80-351 1.32e-23

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.


Pssm-ID: 397722 [Multi-domain]  Cd Length: 259  Bit Score: 100.26  E-value: 1.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793106767  80 GQFTLKDLPKDWGKTITPLMPKTdsktpLKPmlYFIGKYEVTARQYAEVMAQ--------AQSLASGEPAPACEALQAEV 151
Cdd:pfam03781  11 GSFEMGSAERTGNDNEAPAHDVT-----VRP--FAIDKYPVTNAQYAAFVEAtgyttevyPQWWAEVEGANWRHPSGGLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793106767 152 PQGMAGRLPKVKLSRFEAErfsaVYSAWLtkyhkdllpvsGRGTsaeeggLGFVRLPTEVEWEFAARGGQAvsrqeleGR 231
Cdd:pfam03781  84 DIDDGADHPVTGVSWYDAV----AYARWL-----------GKRT------GNGYRLPTEAEWEYAARGGSK-------GR 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793106767 232 LFPRRLEGSEGDGPLADWAVFNQVAGGTGQAARLMPIGTKLPNPIGLFDVIGNAAEMVQESFQLVHAGRRQGAYGGF--- 308
Cdd:pfam03781 136 RYPWGDELYPAGNIWQGADFPNEHAGADSFNGRTSPVGSFPPNALGLYDMAGNVWEWTSDWYKPHYSFAPYDELSRDnfg 215

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2793106767 309 ----VVKGGNYLEGEGTLFtgMRREYPL-FAADGTEQSNetTGFRVAI 351
Cdd:pfam03781 216 ggyrVVRGGSWACSVYPSR--LRPAFRGnCQTPGTRADD--VGFRLVR 259
egtB_TIGR03440 TIGR03440
ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of ...
 206-245 5.01e-03

ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of the ergothioneine biosynthesis, as found in numerous Actinobacteria. Characterized homologs to this family include a formylglycine-generating enzyme that serves as a maturase for an aerobic sulfatase (cf. the radical SAM enzymes that serve as anaerobic sulfatase maturases). [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 274581 [Multi-domain]  Cd Length: 406  Bit Score: 39.62  E-value: 5.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2793106767 206 RLPTEVEWEFAARGGQAVSRQELEGRLFPRRLEGSEGDGP 245
Cdd:TIGR03440 291 RLPTEAEWEKAARWGDAPPNFAEANLGAPVGAYPAGAQGL 330
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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