KEGG   ENZYME: 1.8.3.7Help
Entry
EC 1.8.3.7                  Enzyme                                 

Name
formylglycine-generating enzyme;
sulfatase-modifying factor 1;
Calpha-formylglycine-generating enzyme 1;
SUMF1 (gene name)
Class
Oxidoreductases;
Acting on a sulfur group of donors;
With oxygen as acceptor
BRITE hierarchy
Sysname
[sulfatase]-L-cysteine:oxygen oxidoreductase (3-oxo-L-alanine-forming)
Reaction(IUBMB)
a [sulfatase]-L-cysteine + O2 + 2 a thiol = a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O [RN:R11878]
Reaction(KEGG)
Substrate
[sulfatase]-L-cysteine [CPD:C21740];
O2 [CPD:C00007];
a thiol
Product
[sulfatase]-3-oxo-L-alanine [CPD:C21741];
hydrogen sulfide [CPD:C00283];
disulfide [CPD:C15496];
H2O [CPD:C00001]
Comment
Requires a copper cofactor and Ca2+. The enzyme, which is found in both prokaryotes and eukaryotes, catalyses a modification of a conserved L-cysteine residue in the active site of sulfatases, generating a unique 3-oxo-L-alanine residue that is essential for sulfatase activity. The exact nature of the thiol involved is still not clear - dithiothreitol and cysteamine are the most efficiently used thiols in vitro. Glutathione alo acts in vitro, but it is not known whether it is used in vivo.
History
EC 1.8.3.7 created 2014
Orthology
K13444  formylglycine-generating enzyme
Genes
HSA: 285362(SUMF1)
PTR: 470739(SUMF1)
PPS: 100986538(SUMF1)
GGO: 101150774(SUMF1)
PON: 100446797(SUMF1)
NLE: 100585835(SUMF1)
MCC: 704112(SUMF1)
MCF: 102118800(SUMF1)
CSAB: 103227937(SUMF1)
RRO: 104664268(SUMF1)
RBB: 108528742(SUMF1)
CJC: 100410037(SUMF1)
SBQ: 101029874(SUMF1)
MMU: 58911(Sumf1)
RNO: 362409(Sumf1)
CGE: 100766494(Sumf1)
NGI: 103751201(Sumf1)
HGL: 101704938(Sumf1)
CCAN: 109696829(Sumf1)
OCU: 100346570(SUMF1)
TUP: 102468374(SUMF1)
CFA: 484681(SUMF1)
AML: 105237960(SUMF1)
UMR: 103669599(SUMF1)
ORO: 101368042(SUMF1)
FCA: 101100288(SUMF1)
PTG: 102965850(SUMF1)
AJU: 106978947(SUMF1)
BTA: 536435(SUMF1)
BOM: 102268812(SUMF1)
BIU: 109576370(SUMF1)
PHD: 102324855(SUMF1)
CHX: 102188808(SUMF1)
OAS: 101110003(SUMF1)
SSC: 100514188(SUMF1)
CFR: 102521577(SUMF1)
CDK: 105093157(SUMF1)
BACU: 103009289(SUMF1)
LVE: 103080483(SUMF1)
OOR: 101282162(SUMF1)
ECB: 100052857(SUMF1)
EPZ: 103550290(SUMF1)
EAI: 106848461(SUMF1)
MYB: 102253059(SUMF1)
MYD: 102761335(SUMF1)
HAI: 109395807(SUMF1)
RSS: 109443416(SUMF1)
PALE: 102895225(SUMF1)
LAV: 100661254(SUMF1)
TMU: 101342283
MDO: 100022619(SUMF1)
SHR: 111719439(SUMF1)
OAA: 100092877(SUMF1)
GGA: 100859261(SUMF1)
MGP: 100542598(SUMF1)
CJO: 107319933(SUMF1)
APLA: 101792450(SUMF1)
ACYG: 106036715(SUMF1)
TGU: 100231956(SUMF1)
GFR: 102045152(SUMF1)
FAB: 101817291(SUMF1)
PHI: 102105001(SUMF1)
PMAJ: 107210431(SUMF1)
CCW: 104683392(SUMF1)
FPG: 101920893(SUMF1)
FCH: 102056505(SUMF1)
CLV: 102096028(SUMF1)
EGZ: 104132667(SUMF1)
AAM: 106489802(SUMF1)
ASN: 102379933(SUMF1)
AMJ: 102562381(SUMF1)
PSS: 102462137(SUMF1)
CMY: 102941952(SUMF1)
CPIC: 101946086(SUMF1)
ACS: 100568234(sumf1)
PVT: 110088198(SUMF1)
PBI: 103055327(SUMF1)
GJA: 107121150(SUMF1)
XLA: 432261(sumf1.L)
XTR: 549170(sumf1)
NPR: 108791915(SUMF1)
DRE: 553423(sumf1)
SRX: 107710999(sumf1) 107735668
SGH: 107585117
CCAR: 109078444(sumf1)
IPU: 108271736(sumf1)
AMEX: 103022791(sumf1)
TRU: 101074963(sumf1)
LCO: 104931268(sumf1)
NCC: 104954965(sumf1)
MZE: 101464563(sumf1)
OLA: 101167950(sumf1)
XMA: 102218008(sumf1)
PRET: 103465354(sumf1)
NFU: 107384051(sumf1)
CSEM: 103385990(sumf1)
LCF: 108885993(sumf1)
HCQ: 109522342(sumf1)
BPEC: 110158707(sumf1)
SASA: 100195106(sumf1) 106583142
ELS: 105017007(sumf1)
SFM: 108936900(sumf1)
LCM: 102360608(SUMF1)
CMK: 103185048(sumf1)
CIN: 100187124
SPU: 577665(SUMF1)
APLC: 110986912
SKO: 100371959
DME: Dmel_CG7049(CG7049)
DSI: Dsimw501_GD13538(Dsim_GD13538)
MDE: 101899542
AAG: 5569227
AME: 409298
BIM: 100749607
BTER: 100646854
SOC: 105207375
AEC: 105143045
PBAR: 105431292
HST: 105190154
CFO: 105259017
LHU: 105679937
PGC: 109864061
NVI: 100115827
TCA: 658168
DPA: 109537406
NVL: 108557723
BMOR: 101741318
PMAC: 106716631
API: 100162259
DNX: 107164261
ZNE: 110828418
TUT: 107364195
CRG: 105346705
OBI: 106872187
EPA: 110241933
ADF: 107348220
HMG: 100198082
AQU: 100638921
SMIN: v1.2.036407.t1(symbB.v1.2.036407.t1)
 » show all
Taxonomy
Reference
1  [PMID:9342345]
  Authors
Dierks T, Schmidt B, von Figura K
  Title
Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum.
  Journal
Proc Natl Acad Sci U S A 94:11963-8 (1997)
DOI:10.1073/pnas.94.22.11963
Reference
2  [PMID:9748219]
  Authors
Dierks T, Miech C, Hummerjohann J, Schmidt B, Kertesz MA, von Figura K
  Title
Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine.
  Journal
J Biol Chem 273:25560-4 (1998)
DOI:10.1074/jbc.273.40.25560
Reference
3  [PMID:15657036]
  Authors
Preusser-Kunze A, Mariappan M, Schmidt B, Gande SL, Mutenda K, Wenzel D, von Figura K, Dierks T
  Title
Molecular characterization of the human Calpha-formylglycine-generating enzyme.
  Journal
J Biol Chem 280:14900-10 (2005)
DOI:10.1074/jbc.M413383200
  Sequence
[hsa:285362]
Reference
4  [PMID:16368756]
  Authors
Roeser D, Preusser-Kunze A, Schmidt B, Gasow K, Wittmann JG, Dierks T, von Figura K, Rudolph MG
  Title
A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme.
  Journal
Proc Natl Acad Sci U S A 103:81-6 (2006)
DOI:10.1073/pnas.0507592102
  Sequence
[hsa:285362]
Reference
5  [PMID:18390551]
  Authors
Carlson BL, Ballister ER, Skordalakes E, King DS, Breidenbach MA, Gilmore SA, Berger JM, Bertozzi CR
  Title
Function and structure of a prokaryotic formylglycine-generating enzyme.
  Journal
J Biol Chem 283:20117-25 (2008)
DOI:10.1074/jbc.M800217200
  Sequence
[mtu:Rv0712] [sco:SCO7548]
Reference
6  [PMID:25931126]
  Authors
Holder PG, Jones LC, Drake PM, Barfield RM, Banas S, de Hart GW, Baker J, Rabuka D
  Title
Reconstitution of Formylglycine-generating Enzyme with Copper(II) for Aldehyde Tag Conversion.
  Journal
J Biol Chem 290:15730-45 (2015)
DOI:10.1074/jbc.M115.652669
Reference
7  [PMID:26403223]
  Authors
Knop M, Engi P, Lemnaru R, Seebeck FP
  Title
In Vitro Reconstitution of Formylglycine-Generating Enzymes Requires Copper(I).
  Journal
Chembiochem 16:2147-50 (2015)
DOI:10.1002/cbic.201500322
Reference
8  [PMID:27862795]
  Authors
Knop M, Dang TQ, Jeschke G, Seebeck FP
  Title
Copper is a Cofactor of the Formylglycine-Generating Enzyme.
  Journal
Chembiochem 18:161-165 (2017)
DOI:10.1002/cbic.201600359
Reference
9  [PMID:28544744]
  Authors
Meury M, Knop M, Seebeck FP
  Title
Structural Basis for Copper-Oxygen Mediated C-H Bond Activation by the Formylglycine-Generating Enzyme.
  Journal
Angew Chem Int Ed Engl 56:8115-8119 (2017)
DOI:10.1002/anie.201702901
  Sequence
[tcu:Tcur_4811]
Other DBs
ExplorEnz - The Enzyme Database: 1.8.3.7
IUBMB Enzyme Nomenclature: 1.8.3.7
ExPASy - ENZYME nomenclature database: 1.8.3.7
BRENDA, the Enzyme Database: 1.8.3.7

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