FGE_STRCO
ID FGE_STRCO Reviewed; 314 AA.
AC Q9F3C7;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Formylglycine-generating enzyme {ECO:0000303|PubMed:18390551, ECO:0000303|PubMed:25931126};
DE Short=FGE {ECO:0000303|PubMed:18390551};
DE Short=sc-FGE {ECO:0000303|PubMed:25931126};
DE EC=1.8.3.7 {ECO:0000269|PubMed:25931126};
GN OrderedLocusNames=SCO7548 {ECO:0000312|EMBL:CAC16428.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP COFACTOR.
RX PubMed=25931126; DOI=10.1074/jbc.m115.652669;
RA Holder P.G., Jones L.C., Drake P.M., Barfield R.M., Banas S., de Hart G.W.,
RA Baker J., Rabuka D.;
RT "Reconstitution of formylglycine-generating enzyme with copper(II) for
RT aldehyde tag conversion.";
RL J. Biol. Chem. 290:15730-15745(2015).
RN [3] {ECO:0007744|PDB:2Q17}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 3-314 IN COMPLEX WITH CALCIUM,
RP FUNCTION, PATHWAY, AND MUTAGENESIS OF TRP-234; CYS-272 AND CYS-277.
RX PubMed=18390551; DOI=10.1074/jbc.m800217200;
RA Carlson B.L., Ballister E.R., Skordalakes E., King D.S., Breidenbach M.A.,
RA Gilmore S.A., Berger J.M., Bertozzi C.R.;
RT "Function and structure of a prokaryotic formylglycine-generating enzyme.";
RL J. Biol. Chem. 283:20117-20125(2008).
CC -!- FUNCTION: Oxidase that catalyzes the conversion of cysteine to 3-
CC oxoalanine on target proteins. 3-oxoalanine modification, which is also
CC named formylglycine (fGly), occurs in the maturation of arylsulfatases
CC and some alkaline phosphatases that use the hydrated form of 3-
CC oxoalanine as a catalytic nucleophile. {ECO:0000269|PubMed:18390551,
CC ECO:0000269|PubMed:25931126}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a thiol + L-cysteinyl-[sulfatase] + O2 = 3-oxo-L-alanyl-
CC [sulfatase] + an organic disulfide + H(+) + H2O + hydrogen sulfide;
CC Xref=Rhea:RHEA:51152, Rhea:RHEA-COMP:12900, Rhea:RHEA-COMP:12901,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29256, ChEBI:CHEBI:29919, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:35489, ChEBI:CHEBI:85621; EC=1.8.3.7;
CC Evidence={ECO:0000269|PubMed:25931126};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:25931126};
CC Note=The catalytic copper is required to activate oxygen and catalyze
CC oxidative C-H activation. {ECO:0000269|PubMed:25931126};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=96 uM for [sulfatase]-L-cysteine {ECO:0000269|PubMed:25931126};
CC Note=kcat is 17.3 min(-1) with [sulfatase]-L-cysteine as substrate.
CC {ECO:0000269|PubMed:25931126};
CC -!- PATHWAY: Protein modification; sulfatase oxidation.
CC {ECO:0000269|PubMed:18390551, ECO:0000269|PubMed:25931126}.
CC -!- SIMILARITY: Belongs to the sulfatase-modifying factor family.
CC {ECO:0000305}.
CC -!- CAUTION: The disulfide bond observed in the structure does not exist in
CC vivo (PubMed:18390551). The enzyme reaction was initially thought to
CC act via a redox-active disulfide bond mechanism; however the disulfide
CC bond only takes place with inactive enzyme that lacks the copper
CC cofactor (PubMed:25931126). The catalytic copper is required to
CC activate oxygen and catalyze oxidative C-H activation
CC (PubMed:25931126). {ECO:0000269|PubMed:18390551,
CC ECO:0000269|PubMed:25931126}.
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DR EMBL; AL939132; CAC16428.1; -; Genomic_DNA.
DR RefSeq; NP_631591.1; NC_003888.3.
DR RefSeq; WP_011031741.1; NZ_VNID01000005.1.
DR PDB; 2Q17; X-ray; 2.10 A; A/B/C/D/E=3-314.
DR PDB; 6MUJ; X-ray; 2.25 A; A/B/C/D/E=2-314.
DR PDBsum; 2Q17; -.
DR PDBsum; 6MUJ; -.
DR AlphaFoldDB; Q9F3C7; -.
DR SMR; Q9F3C7; -.
DR STRING; 100226.SCO7548; -.
DR GeneID; 1102986; -.
DR KEGG; sco:SCO7548; -.
DR PATRIC; fig|100226.15.peg.7662; -.
DR eggNOG; COG1262; Bacteria.
DR HOGENOM; CLU_012431_4_2_11; -.
DR InParanoid; Q9F3C7; -.
DR OMA; EWEYAGK; -.
DR PhylomeDB; Q9F3C7; -.
DR BRENDA; 1.8.3.7; 5998.
DR UniPathway; UPA00910; -.
DR EvolutionaryTrace; Q9F3C7; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:1903135; F:cupric ion binding; IDA:UniProtKB.
DR GO; GO:0120147; F:Formylglycine-generating oxidase activity; IDA:UniProtKB.
DR GO; GO:0043687; P:post-translational protein modification; IDA:UniProtKB.
DR GO; GO:0018158; P:protein oxidation; IDA:UniProtKB.
DR Gene3D; 3.90.1580.10; -; 1.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR005532; SUMF_dom.
DR InterPro; IPR042095; SUMF_sf.
DR Pfam; PF03781; FGE-sulfatase; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Copper; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..314
FT /note="Formylglycine-generating enzyme"
FT /id="PRO_0000444617"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18390551,
FT ECO:0007744|PDB:2Q17"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18390551,
FT ECO:0007744|PDB:2Q17"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18390551,
FT ECO:0007744|PDB:2Q17"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18390551,
FT ECO:0007744|PDB:2Q17"
FT BINDING 272
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:25931126"
FT BINDING 277
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:25931126"
FT MUTAGEN 234
FT /note="W->A,F: Does not abolish formylglycine-generating
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:18390551"
FT MUTAGEN 272
FT /note="C->S: Abolished formylglycine-generating enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:18390551"
FT MUTAGEN 277
FT /note="C->S: Abolished formylglycine-generating enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:18390551"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:2Q17"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2Q17"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:2Q17"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:2Q17"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:2Q17"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:2Q17"
FT HELIX 84..88
FT /evidence="ECO:0007829|PDB:2Q17"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:2Q17"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:2Q17"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2Q17"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:2Q17"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:2Q17"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:2Q17"
FT HELIX 163..171
FT /evidence="ECO:0007829|PDB:2Q17"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:2Q17"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:2Q17"
FT STRAND 229..240
FT /evidence="ECO:0007829|PDB:2Q17"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:2Q17"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:2Q17"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:2Q17"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:2Q17"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:2Q17"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:2Q17"
SQ SEQUENCE 314 AA; 33736 MW; E0F4B2A3E0F412F5 CRC64;
MAVAAPSPAA AAEPGPAARP RSTRGQVRLP GGEFAMGDAF GEGYPADGET PVHTVRLRPF
HIDETAVTNA RFAAFVKATG HVTDAERFGS SAVFHLVVAA PDADVLGSAA GAPWWINVRG
AHWRRPEGAR SDITGRPNHP VVHVSWNDAT AYARWAGKRL PTEAEWEYAA RGGLAGRRYA
WGDELTPGGR WRCNIWQGRF PHVNTAEDGH LSTAPVKSYR PNGHGLWNTA GNVWEWCSDW
FSPTYYAESP TVDPHGPGTG AARVLRGGSY LCHDSYCNRY RVAARSSNTP DSSSGNLGFR
CANDADLTSG SAAE
