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Conserved domains on  [gi|2797051736|ref|WP_373365879|]
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formylglycine-generating enzyme family protein [Pseudomonas syringae]

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
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 ...
57-272 1.50e-28

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: 112.79  E-value: 1.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797051736  57 GSFTNEKDAKSRY---YLLAKYEMTALQYSALTQA------ECPTPSNKQR--LPIVSLSWiqamDAADKYNVWLRenaa 125
Cdd:COG1262    30 GAFDNERPRHRVTvspFYIDKYEVTNAEYRAFVGWtladgrNNPLYSDFGGpdHPVVHVSW----YDAQAYCRWLG---- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797051736 126 dklpKEDGIagFLRLPTEVEWEFAARGGlsvstaefRDLRYPMPEGLNA-YEWFAGtQSSNGQLQLAGLLKPNPLGLHDM 204
Cdd:COG1262   102 ----KKTGK--GYRLPTEAEWEYAARGG--------DGRPYPWGDDLPPeLANYAG-NDGRGSTAPVGSFPPNPFGLYDM 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2797051736 205 LGNVDEMMFEPFRLNKLDRQH------GQAGGYVVRGGDYRTAQGELRSSLrkeRNYYDakAAATSKTTGVRLA 272
Cdd:COG1262   167 AGNVWEWTADWYDPPYPGAPAdgpvgpENGGQRVLRGGSWATPPDHLRSAY---RNFFP--PDARWQFVGFRLA 235
 
Name Accession Description Interval E-value
YfmG COG1262
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain ...
57-272 1.50e-28

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: 112.79  E-value: 1.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797051736  57 GSFTNEKDAKSRY---YLLAKYEMTALQYSALTQA------ECPTPSNKQR--LPIVSLSWiqamDAADKYNVWLRenaa 125
Cdd:COG1262    30 GAFDNERPRHRVTvspFYIDKYEVTNAEYRAFVGWtladgrNNPLYSDFGGpdHPVVHVSW----YDAQAYCRWLG---- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797051736 126 dklpKEDGIagFLRLPTEVEWEFAARGGlsvstaefRDLRYPMPEGLNA-YEWFAGtQSSNGQLQLAGLLKPNPLGLHDM 204
Cdd:COG1262   102 ----KKTGK--GYRLPTEAEWEYAARGG--------DGRPYPWGDDLPPeLANYAG-NDGRGSTAPVGSFPPNPFGLYDM 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2797051736 205 LGNVDEMMFEPFRLNKLDRQH------GQAGGYVVRGGDYRTAQGELRSSLrkeRNYYDakAAATSKTTGVRLA 272
Cdd:COG1262   167 AGNVWEWTADWYDPPYPGAPAdgpvgpENGGQRVLRGGSWATPPDHLRSAY---RNFFP--PDARWQFVGFRLA 235
FGE-sulfatase pfam03781
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
91-272 1.65e-28

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: 113.36  E-value: 1.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797051736  91 PTPSNKQRLPIVSLSWiqamDAADKYNVWLRENAAdklpkedgiaGFLRLPTEVEWEFAARGGLSVSTAEFRDLRYP--- 167
Cdd:pfam03781  83 SDIDDGADHPVTGVSW----YDAVAYARWLGKRTG----------NGYRLPTEAEWEYAARGGSKGRRYPWGDELYPagn 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797051736 168 MPEGLNAYEWFAGTQSSNGQLQLAGLLKPNPLGLHDMLGNVDEMMFEPFRL-------NKLDRQHGQAGGYVVRGGDYRT 240
Cdd:pfam03781 149 IWQGADFPNEHAGADSFNGRTSPVGSFPPNALGLYDMAGNVWEWTSDWYKPhysfapyDELSRDNFGGGYRVVRGGSWAC 228
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2797051736 241 AqgELRSSLRKERNYYDAKAAATSKTTGVRLA 272
Cdd:pfam03781 229 S--VYPSRLRPAFRGNCQTPGTRADDVGFRLV 258
egtB_TIGR03440 TIGR03440
ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of ...
139-250 5.44e-06

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: 48.48  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797051736 139 RLPTEVEWEFAARGGLSvstaefrdlrypmpeglnayewfAGTQSSNGQLQLAGLLKPNPLGLHDMLGNVDEMM------ 212
Cdd:TIGR03440 291 RLPTEAEWEKAARWGDA-----------------------PPNFAEANLGAPVGAYPAGAQGLGQLFGDVWEWTaspyep 347
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2797051736 213 ---FEPFRlnkldrqhGQAGGY---------VVRGGDYRTAQGELRSSLR 250
Cdd:TIGR03440 348 ypgFRPPP--------GAYGEYngkfmdgqmVLRGGSCATPPRHLRPSYR 389
 
Name Accession Description Interval E-value
YfmG COG1262
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain ...
57-272 1.50e-28

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: 112.79  E-value: 1.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797051736  57 GSFTNEKDAKSRY---YLLAKYEMTALQYSALTQA------ECPTPSNKQR--LPIVSLSWiqamDAADKYNVWLRenaa 125
Cdd:COG1262    30 GAFDNERPRHRVTvspFYIDKYEVTNAEYRAFVGWtladgrNNPLYSDFGGpdHPVVHVSW----YDAQAYCRWLG---- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797051736 126 dklpKEDGIagFLRLPTEVEWEFAARGGlsvstaefRDLRYPMPEGLNA-YEWFAGtQSSNGQLQLAGLLKPNPLGLHDM 204
Cdd:COG1262   102 ----KKTGK--GYRLPTEAEWEYAARGG--------DGRPYPWGDDLPPeLANYAG-NDGRGSTAPVGSFPPNPFGLYDM 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2797051736 205 LGNVDEMMFEPFRLNKLDRQH------GQAGGYVVRGGDYRTAQGELRSSLrkeRNYYDakAAATSKTTGVRLA 272
Cdd:COG1262   167 AGNVWEWTADWYDPPYPGAPAdgpvgpENGGQRVLRGGSWATPPDHLRSAY---RNFFP--PDARWQFVGFRLA 235
FGE-sulfatase pfam03781
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
91-272 1.65e-28

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: 113.36  E-value: 1.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797051736  91 PTPSNKQRLPIVSLSWiqamDAADKYNVWLRENAAdklpkedgiaGFLRLPTEVEWEFAARGGLSVSTAEFRDLRYP--- 167
Cdd:pfam03781  83 SDIDDGADHPVTGVSW----YDAVAYARWLGKRTG----------NGYRLPTEAEWEYAARGGSKGRRYPWGDELYPagn 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797051736 168 MPEGLNAYEWFAGTQSSNGQLQLAGLLKPNPLGLHDMLGNVDEMMFEPFRL-------NKLDRQHGQAGGYVVRGGDYRT 240
Cdd:pfam03781 149 IWQGADFPNEHAGADSFNGRTSPVGSFPPNALGLYDMAGNVWEWTSDWYKPhysfapyDELSRDNFGGGYRVVRGGSWAC 228
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2797051736 241 AqgELRSSLRKERNYYDAKAAATSKTTGVRLA 272
Cdd:pfam03781 229 S--VYPSRLRPAFRGNCQTPGTRADDVGFRLV 258
egtB_TIGR03440 TIGR03440
ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of ...
139-250 5.44e-06

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: 48.48  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2797051736 139 RLPTEVEWEFAARGGLSvstaefrdlrypmpeglnayewfAGTQSSNGQLQLAGLLKPNPLGLHDMLGNVDEMM------ 212
Cdd:TIGR03440 291 RLPTEAEWEKAARWGDA-----------------------PPNFAEANLGAPVGAYPAGAQGLGQLFGDVWEWTaspyep 347
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2797051736 213 ---FEPFRlnkldrqhGQAGGY---------VVRGGDYRTAQGELRSSLR 250
Cdd:TIGR03440 348 ypgFRPPP--------GAYGEYngkfmdgqmVLRGGSCATPPRHLRPSYR 389
 
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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