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)
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)
SCAN: 103823695(SUMF1)
GFR: 102045152(SUMF1)
FAB: 101817291(SUMF1)
PHI: 102105001(SUMF1)
PMAJ: 107210431(SUMF1)
CCAE: 111934935(SUMF1)
CCW: 104683392(SUMF1)
FPG: 101920893(SUMF1)
FCH: 102056505(SUMF1)
CLV: 102096028(SUMF1)
EGZ: 104132667(SUMF1)
NNI: 104017009(SUMF1)
ACUN: 113484758(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)
PMUR: 107296296(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)
PHYP: 113545901(sumf1)
AMEX: 103022791(sumf1)
EEE: 113575976(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)
KMR: 108235606(sumf1)
CSEM: 103385990(sumf1)
LCF: 108885993(sumf1)
SDU: 111221797(sumf1)
HCQ: 109522342(sumf1)
BPEC: 110158707(sumf1)
MALB: 109956229(sumf1)
SASA: 100195106(sumf1) 106583142
OTW: 112216866(sumf1)
SALP: 111966187(sumf1)
ELS: 105017007(sumf1)
SFM: 108936900(sumf1)
PKI: 111840591(sumf1)
LCM: 102360608(SUMF1)
CMK: 103185048(sumf1)
CIN: 100187124
SPU: 577665(SUMF1)
APLC: 110986912
SKO: 100371959
DME: Dmel_CG7049(CG7049)
DER: 6544639
DPE: 6601052
DSI: Dsimw501_GD13538(Dsim_GD13538)
DWI: 6643041
MDE: 101899542
AAG: 5569227
AME: 409298
BIM: 100749607
BTER: 100646854
SOC: 105207375
MPHA: 105839259
AEC: 105143045
PBAR: 105431292
HST: 105190154
DQU: 106747670
CFO: 105259017
LHU: 105679937
PGC: 109864061
OBO: 105286235
PCF: 106785538
NVI: 100115827
MDL: 103573724
TCA: 658168
DPA: 109537406
NVL: 108557723
BMOR: 101741318
PMAC: 106716631
HAW: 110375229
TNL: 113502722
API: 100162259
DNX: 107164261
CLEC: 106671132
ZNE: 110828418
TUT: 107364195
DPTE: 113792098
CRG: 105346705
OBI: 106872187
EPA: 110241933
ADF: 107348220
PDAM: 113668561
SPIS: 111337648
HMG: 100198082
AQU: 100638921
SMIN: v1.2.036407.t1(symbB.v1.2.036407.t1)
ETE: ETEE_0995
PPU: PP_3353
PPF: Pput_2405
PPI: ND018
PPX: T1E_5508
PPUT: L483_20030
PSEM: TO66_13435
ACB: A1S_0976
ABY: ABAYE2816
ABN: AB57_1055
ABX: ABK1_0963
ABH: M3Q_1275
ABAD: ABD1_09300
ABAA: IX88_06900
ACC: BDGL_000256(sumF1) BDGL_000398(sumF1)
GNI: GNIT_2489
GAI: IMCC3135_00900(pkn1_1) IMCC3135_05980(pkn1_2) IMCC3135_09550(pkn1_3)
REH: H16_A1600(h16_A1600)
RME: Rmet_4529(sumF1) Rmet_5422(sumF)
BCN: Bcen_5208
BCJ: BCAM0570
BCEN: DM39_4591
BCEW: DM40_3634
BCEO: I35_4465
BMU: Bmul_5129
BMK: DM80_4307
BMUL: NP80_3588
BDL: AK34_4842
BCON: NL30_22945
BUB: BW23_4290
BLAT: WK25_20760
BTEI: WS51_01450
BSEM: WJ12_22850
BPSL: WS57_11015
BMEC: WJ16_21865
BSTG: WT74_21875
BGO: BM43_5192
BXE: Bxe_A2134
BXB: DR64_4289
BPA: BPP2758
BPAR: BN117_2528
BBR: BB2727
AXX: ERS451415_03672(pkn1_2)
AFQ: AFA_05700
ACRA: BSY15_2782
MPT: Mpe_A2681
MMS: mma_2409
CFU: CFU_0043
AZA: AZKH_0377
BPRC: D521_0648
MXA: MXAN_3662
BBAT: Bdt_1435
BBAC: EP01_03505
MLO: mll5466
PLA: Plav_1132
RBS: RHODOSMS8_02769(pkn1)
SME: SM_b20334
SMD: Smed_3787
ARA: Arad_7818
BRAD: BF49_0675
NHA: Nham_2985
XAU: Xaut_4691
AZC: AZC_2860
MDI: METDI0903
MNO: Mnod_8069
MOR: MOC_3701
MSL: Msil_3121
HDN: Hden_2938
PHL: KKY_1245
PLEO: OHA_1_02151(pkn1_1)
MMED: Mame_02010(pkn1)
CCR: CC_1173
CAK: Caul_2673
CSE: Cseg_2708
OTM: OSB_05700(pkn1)
MALG: MALG_03903
HNE: HNE_1666
GAK: X907_2604
SAL: Sala_0300
SMAZ: LH19_12305
SPHU: SPPYR_0446(Sumf) SPPYR_3584(Sumf)
SWI: Swit_1048
SPHD: HY78_21265
SPHM: G432_12910
STAX: MC45_15925
SPKC: KC8_09655
SPMI: K663_16330
SPHR: BSY17_3201
SINB: SIDU_15100
SPHT: K426_22419
ANH: A6F65_00918(pkn1)
ADO: A6F68_02507(pkn1)
GOH: B932_3174
PSWU: SY83_12470
SPW: SPCG_1784
SJJ: SPJ_1707
SPX: SPG_1694
SPV: SPH_1923
SPP: SPP_1806
SNP: SPAP_1797
LCB: LCABL_03770(zgc:136465)
LCS: LCBD_0379
LCE: LC2W_0375
LCW: BN194_03840(Sumf1)
ECAS: ECBG_00347
MTU: Rv0712
MTV: RVBD_0712
MTC: MT0739
MRA: MRA_0720
MTUR: CFBS_0748
MTD: UDA_0712
MTUC: J113_05025
MTUE: J114_03800
MTUH: I917_05040
MTUL: TBHG_00706
MTUT: HKBT1_0748
MTUU: HKBT2_0749
MBB: BCG_0762
MBT: JTY_0732
MAF: MAF_07210
MMIC: RN08_0792
MPA: MAP_4174
MAO: MAP4_4299
MAVI: RC58_21355
MAVU: RE97_21405
MIT: OCO_43500
MIA: OCU_43260
MID: MIP_06602
MYO: OEM_43730
MIR: OCQ_44610
MUL: MUL_0225
MMM: W7S_21930
MHAD: B586_18695
MSHG: MSG_00920
MGI: Mflv_5038
MPHL: MPHLCCUG_01320(pkn1)
MTHN: 4412656_00965(pkn1)
MHAS: MHAS_00244(pkn1)
MAB: MAB_4305
MABB: MASS_4346
MCHE: BB28_22225
MSTE: MSTE_04490
MTER: 4434518_03312(pkn1)
CEF: CE1569
RER: RER_45110
REY: O5Y_21225
REQ: REQ_18030
RRT: 4535765_02470(pkn1)
GOR: KTR9_1487
GRU: GCWB2_07795(pkn1)
GOM: D7316_02693(pkn1_1) D7316_03915(pkn1_2)
TPR: Tpau_3335
SCO: SCO7548(SC5F1.02)
SALS: SLNWT_4756
STRP: F750_0878
SFI: SFUL_1341
SLV: SLIV_01570(sumF)
SLD: T261_0126
STRM: M444_15435
SPRI: SPRI_1484
STRD: NI25_35920
SMAL: SMALA_0381
SLX: SLAV_07100(pkn1)
KSK: KSE_71910
ART: Arth_1714
ARM: ART_4158
AAU: AAur_1451
LMOI: VV02_15390
SERJ: SGUI_2049
BLIN: BLSMQ_0655
MPH: MLP_36420
NDK: I601_0861(pkn1)
TCU: Tcur_4811
SRO: Sros_3062
SEN: SACE_3100
PDX: Psed_0726
ALO: CRK56739
MIL: ML5_3220
ASE: ACPL_2486
ACTS: ACWT_2359
SNA: Snas_0111
CWO: Cwoe_3066
SYNR: KR49_13830
PMT: PMT_1516
CYT: cce_1566
CALH: IJ00_08845
TAQ: TO73_2398
PNL: PNK_2368
PUV: PUV_21530(sUMF1)
OBG: Verru16b_00236(pkn1_1) Verru16b_02686(pkn1_4) Verru16b_02687(pkn1_5)
PIR: VN12_19420(pkn1_3)
PLM: Plim_0932
PLS: VT03_00575(pkn1_1) VT03_09440(pkn1_3) VT03_14660(pkn1_4)
PLH: VT85_17180(pkn1_4)
FMR: Fuma_05168(pkn1_5)
GES: VT84_36085(pkn1_9)
IPA: Isop_3638
PBOR: BSF38_03283(pkn1_3)
PBU: L21SP3_00042(pkn1_1) L21SP3_00477(pkn1_2) L21SP3_01440(pkn1_3) L21SP3_01714(pkn1_5) L21SP3_02018(pkn1_6)
PBP: STSP1_00485(pkn1_1) STSP1_00959(pkn1_2) STSP1_01091(pkn1_3) STSP1_01795(pkn1_5) STSP1_02105(pkn1_6)
LIE: LIF_A2522
LIS: LIL_12653
SUS: Acid_7564
GBA: J421_0702
MBAS: ALGA_3944
CPI: Cpin_1837
SGN: SGRA_3527
PHE: Phep_0378
SMIZ: 4412673_03421(pkn1_4)
DFE: Dfer_3179
SLI: Slin_1433
FAE: FAES_4663
GFO: GFO_2087
GFL: GRFL_0152
FJO: Fjoh_2206
FJG: BB050_00438(pkn1_1)
ZPR: ZPR_2997
MARM: YQ22_01110
CBAL: M667_10725
CBAT: M666_10730
ZGA: ZOBELLIA_155(fgeA)
MLT: VC82_930
EAO: BD94_0730
ELB: VO54_01944(pkn1)
MARF: CJ739_2215
IAL: IALB_0965
 » 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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