FGE_MYCTU
ID FGE_MYCTU Reviewed; 299 AA.
AC I6Y8I5;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Formylglycine-generating enzyme {ECO:0000303|PubMed:18390551};
DE Short=FGE {ECO:0000303|PubMed:18390551};
DE EC=1.8.3.7 {ECO:0000250|UniProtKB:D1A7C3};
GN OrderedLocusNames=Rv0712 {ECO:0000312|EMBL:CCP43456.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, PATHWAY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-260;
RP CYS-263 AND CYS-268.
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 -!- 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:0000250|UniProtKB:D1A7C3};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:D1A7C3};
CC Note=The catalytic copper is required to activate oxygen and catalyze
CC oxidative C-H activation. {ECO:0000250|UniProtKB:D1A7C3};
CC -!- PATHWAY: Protein modification; sulfatase oxidation.
CC {ECO:0000269|PubMed:18390551}.
CC -!- DISRUPTION PHENOTYPE: Cells are viable and do not display growth
CC defects. They however show reduced sulfatase activity.
CC {ECO:0000269|PubMed:18390551}.
CC -!- SIMILARITY: Belongs to the sulfatase-modifying factor family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP43456.1; -; Genomic_DNA.
DR RefSeq; NP_215226.1; NC_000962.3.
DR RefSeq; WP_003403610.1; NZ_NVQJ01000007.1.
DR AlphaFoldDB; I6Y8I5; -.
DR SMR; I6Y8I5; -.
DR STRING; 83332.Rv0712; -.
DR PaxDb; I6Y8I5; -.
DR PRIDE; I6Y8I5; -.
DR DNASU; 888346; -.
DR GeneID; 888346; -.
DR KEGG; mtu:Rv0712; -.
DR PATRIC; fig|83332.111.peg.788; -.
DR TubercuList; Rv0712; -.
DR eggNOG; COG1262; Bacteria.
DR OMA; WTADLWD; -.
DR PhylomeDB; I6Y8I5; -.
DR BRENDA; 1.8.3.7; 3445.
DR UniPathway; UPA00910; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0120147; F:Formylglycine-generating oxidase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Copper; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..299
FT /note="Formylglycine-generating enzyme"
FT /id="PRO_0000444619"
FT BINDING 263
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:D1A7C3"
FT BINDING 268
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:D1A7C3"
FT MUTAGEN 260
FT /note="S->A: Strongly reduced formylglycine-generating
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:18390551"
FT MUTAGEN 263
FT /note="C->S: Abolished formylglycine-generating enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:18390551"
FT MUTAGEN 268
FT /note="C->S: Abolished formylglycine-generating enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:18390551"
SQ SEQUENCE 299 AA; 32744 MW; BB06E071070AC02D CRC64;
MLTELVDLPG GSFRMGSTRF YPEEAPIHTV TVRAFAVERH PVTNAQFAEF VSATGYVTVA
EQPLDPGLYP GVDAADLCPG AMVFCPTAGP VDLRDWRQWW DWVPGACWRH PFGRDSDIAD
RAGHPVVQVA YPDAVAYARW AGRRLPTEAE WEYAARGGTT ATYAWGDQEK PGGMLMANTW
QGRFPYRNDG ALGWVGTSPV GRFPANGFGL LDMIGNVWEW TTTEFYPHHR IDPPSTACCA
PVKLATAADP TISQTLKGGS HLCAPEYCHR YRPAARSPQS QDTATTHIGF RCVADPVSG
