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Conserved domains on  [gi|691130973|ref|WP_032046197|]
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MULTISPECIES: SUMF1/EgtB/PvdO family nonheme iron enzyme [Acinetobacter]

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 ...
 51-267 6.04e-47

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: 158.24  E-value: 6.04e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691130973  51 DKTKKNLVEIKGGTFMMGDFGEQKSPDklpydsdaDSKPLHKVTLDNYALSATKATYADFDIYTEVTGQEkiGKFDELSI 130
Cdd:COG1262    7 NAVGLEMVLIPGGTFLMGSPEGEGAFD--------NERPRHRVTVSPFYIDKYEVTNAEYRAFVGWTLAD--GRNNPLYS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691130973 131 QDRLPNS-AAGVNWQQARNYCQWLGKQLNLKMDLPTEAQWEYAARNRGQYIlYPTDNGKIDTGRNVWSFEQRQKQQnkln 209
Cdd:COG1262   77 DFGGPDHpVVHVSWYDAQAYCRWLGKKTGKGYRLPTEAEWEYAARGGDGRP-YPWGDDLPPELANYAGNDGRGSTA---- 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 691130973 210 afrnipELMKFPATPLGLYDMITDNYEWMLDWYDPqYYSKSPEKNPQGPAKGSLKVVR 267
Cdd:COG1262  152 ------PVGSFPPNPFGLYDMAGNVWEWTADWYDP-PYPGAPADGPVGPENGGQRVLR 202
 
Name Accession Description Interval E-value
YfmG COG1262
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain ...
 51-267 6.04e-47

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: 158.24  E-value: 6.04e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691130973  51 DKTKKNLVEIKGGTFMMGDFGEQKSPDklpydsdaDSKPLHKVTLDNYALSATKATYADFDIYTEVTGQEkiGKFDELSI 130
Cdd:COG1262    7 NAVGLEMVLIPGGTFLMGSPEGEGAFD--------NERPRHRVTVSPFYIDKYEVTNAEYRAFVGWTLAD--GRNNPLYS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691130973 131 QDRLPNS-AAGVNWQQARNYCQWLGKQLNLKMDLPTEAQWEYAARNRGQYIlYPTDNGKIDTGRNVWSFEQRQKQQnkln 209
Cdd:COG1262   77 DFGGPDHpVVHVSWYDAQAYCRWLGKKTGKGYRLPTEAEWEYAARGGDGRP-YPWGDDLPPELANYAGNDGRGSTA---- 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 691130973 210 afrnipELMKFPATPLGLYDMITDNYEWMLDWYDPqYYSKSPEKNPQGPAKGSLKVVR 267
Cdd:COG1262  152 ------PVGSFPPNPFGLYDMAGNVWEWTADWYDP-PYPGAPADGPVGPENGGQRVLR 202
FGE-sulfatase pfam03781
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
 57-267 9.36e-37

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: 132.62  E-value: 9.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691130973   57 LVEIKGGTFMMGdfgeqkSPDKLPYDSDAdskPLHKVTLDNYALSATKATYADFDIYTEVTG------------------ 118
Cdd:pfam03781   5 MVLIPGGSFEMG------SAERTGNDNEA---PAHDVTVRPFAIDKYPVTNAQYAAFVEATGyttevypqwwaeveganw 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691130973  119 QEKIGKFDELSIQDRLPnsAAGVNWQQARNYCQWLGKQLNLKMDLPTEAQWEYAARNrGQYILYPTDNGKIDTGRNVWSF 198
Cdd:pfam03781  76 RHPSGGLSDIDDGADHP--VTGVSWYDAVAYARWLGKRTGNGYRLPTEAEWEYAARG-GSKGRRYPWGDELYPAGNIWQG 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691130973  199 EQRQKQQNKLNAFRNIPE-LMKFPATPLGLYDMITDNYEWMLDWYDPQYYSKSPEKNPQGPAKGSLKVVR 267
Cdd:pfam03781 153 ADFPNEHAGADSFNGRTSpVGSFPPNALGLYDMAGNVWEWTSDWYKPHYSFAPYDELSRDNFGGGYRVVR 222
egtB_TIGR03440 TIGR03440
ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of ...
 138-244 4.84e-07

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: 50.79  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691130973  138 AAGVNWQQARNYCQWLGKqlnlkmDLPTEAQWEYAARnrgqyilyptdngkidtgrnvWSFEQRQKQQNKLNAFRNIPel 217
Cdd:TIGR03440 273 VCHVSYYEADAYARWAGA------RLPTEAEWEKAAR---------------------WGDAPPNFAEANLGAPVGAY-- 323

                          90       100
                  ....*....|....*....|....*..
gi 691130973  218 mkfPATPLGLYDMITDNYEWMLDWYDP 244
Cdd:TIGR03440 324 ---PAGAQGLGQLFGDVWEWTASPYEP 347
 
Name Accession Description Interval E-value
YfmG COG1262
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain ...
 51-267 6.04e-47

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: 158.24  E-value: 6.04e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691130973  51 DKTKKNLVEIKGGTFMMGDFGEQKSPDklpydsdaDSKPLHKVTLDNYALSATKATYADFDIYTEVTGQEkiGKFDELSI 130
Cdd:COG1262    7 NAVGLEMVLIPGGTFLMGSPEGEGAFD--------NERPRHRVTVSPFYIDKYEVTNAEYRAFVGWTLAD--GRNNPLYS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691130973 131 QDRLPNS-AAGVNWQQARNYCQWLGKQLNLKMDLPTEAQWEYAARNRGQYIlYPTDNGKIDTGRNVWSFEQRQKQQnkln 209
Cdd:COG1262   77 DFGGPDHpVVHVSWYDAQAYCRWLGKKTGKGYRLPTEAEWEYAARGGDGRP-YPWGDDLPPELANYAGNDGRGSTA---- 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 691130973 210 afrnipELMKFPATPLGLYDMITDNYEWMLDWYDPqYYSKSPEKNPQGPAKGSLKVVR 267
Cdd:COG1262  152 ------PVGSFPPNPFGLYDMAGNVWEWTADWYDP-PYPGAPADGPVGPENGGQRVLR 202
FGE-sulfatase pfam03781
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
 57-267 9.36e-37

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: 132.62  E-value: 9.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691130973   57 LVEIKGGTFMMGdfgeqkSPDKLPYDSDAdskPLHKVTLDNYALSATKATYADFDIYTEVTG------------------ 118
Cdd:pfam03781   5 MVLIPGGSFEMG------SAERTGNDNEA---PAHDVTVRPFAIDKYPVTNAQYAAFVEATGyttevypqwwaeveganw 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691130973  119 QEKIGKFDELSIQDRLPnsAAGVNWQQARNYCQWLGKQLNLKMDLPTEAQWEYAARNrGQYILYPTDNGKIDTGRNVWSF 198
Cdd:pfam03781  76 RHPSGGLSDIDDGADHP--VTGVSWYDAVAYARWLGKRTGNGYRLPTEAEWEYAARG-GSKGRRYPWGDELYPAGNIWQG 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691130973  199 EQRQKQQNKLNAFRNIPE-LMKFPATPLGLYDMITDNYEWMLDWYDPQYYSKSPEKNPQGPAKGSLKVVR 267
Cdd:pfam03781 153 ADFPNEHAGADSFNGRTSpVGSFPPNALGLYDMAGNVWEWTSDWYKPHYSFAPYDELSRDNFGGGYRVVR 222
egtB_TIGR03440 TIGR03440
ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of ...
 138-244 4.84e-07

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: 50.79  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 691130973  138 AAGVNWQQARNYCQWLGKqlnlkmDLPTEAQWEYAARnrgqyilyptdngkidtgrnvWSFEQRQKQQNKLNAFRNIPel 217
Cdd:TIGR03440 273 VCHVSYYEADAYARWAGA------RLPTEAEWEKAAR---------------------WGDAPPNFAEANLGAPVGAY-- 323

                          90       100
                  ....*....|....*....|....*..
gi 691130973  218 mkfPATPLGLYDMITDNYEWMLDWYDP 244
Cdd:TIGR03440 324 ---PAGAQGLGQLFGDVWEWTASPYEP 347
 
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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