KEGG   ENZYME: 1.1.98.7
Entry
EC 1.1.98.7                 Enzyme                                 
Name
serine-type anaerobic sulfatase-maturating enzyme;
atsB (gene name)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With other, known, physiological acceptors
Sysname
[sulfatase]-L-serine:S-adenosyl-L-methionine oxidoreductase (3-oxo-L-alanine-forming)
Reaction(IUBMB)
S-adenosyl-L-methionine + a [sulfatase]-L-serine = a [sulfatase]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine [RN:R12569]
Reaction(KEGG)
R12569
Substrate
S-adenosyl-L-methionine [CPD:C00019];
[sulfatase]-L-serine [CPD:C22227]
Product
[sulfatase]-3-oxo-L-alanine [CPD:C21741];
5'-deoxyadenosine [CPD:C05198];
L-methionine [CPD:C00073]
Comment
A bacterial radical S-adenosyl-L-methionine (AdoMet) enzyme that contains three [4Fe-4S] clusters. The enzyme, found in some bacteria, activates a type I sulfatase enzyme (EC 3.1.6.1) by converting a conserved L-serine residue in the active site to a unique 3-oxo-L-alanine residue that is essential for the sulfatase activity. While the enzyme from Klebsiella pneumoniae is specific for L-serine, the enzyme from Clostridium perfringens can also act on L-cysteine, see EC 1.8.98.7, cysteine-type anaerobic sulfatase-maturating enzyme.
History
EC 1.1.98.7 created 2020
Orthology
K24118  serine-type anaerobic sulfatase-maturating enzyme
Genes
STMSTM3123
SEOSTM14_3772
SEVSTMMW_30831
SEYSL1344_3097
SEMSTMDT12_C31760
SEJSTMUK_3111
SEBSTM474_3272
SEFUMN798_3393
SETUSTU288_15805
SETCCFSAN001921_01410
SENRSTMDT2_30171
SENDDT104_31191
SENICY43_16280
SEENSE451236_21730
SPQSPAB_03893
SEISPC_3190
SECSCH_3063(arsR)
SEHSeHA_C3365
SHBSU5_03621
SENHCFSAN002069_16535
SEEHSEEH1578_01740
SEESNSL254_A3372
SENNSN31241_42470
SEWSeSA_A3298
SEDSeD_A3467
SEGSG3017
SELSPUL_3126
SEGASPUCDC_3112
SETSEN2966
SENAAU38_15075
SENOAU37_15085
SENVAU39_15080
SENQAU40_16995
SENLIY59_15685
SENJCFSAN001992_17960
SEEBSEEB0189_004265
SEEPI137_14940
SENBBN855_31950
SENEIA1_15075
SESSARI_04508
SALZEOS98_03705
KPNKPN_00528
KPUKP1_1454
KPMKPHS_13460
KPPA79E_3722
KPHKPNIH24_22060
KPZKPNIH27_06265
KPVKPNIH29_06935
KPWKPNIH30_06945
KPYKPNIH31_06850
KPGKPNIH32_07050
KPCKPNIH10_06745
KPQKPR0928_06660
KPTVK055_2015
KPOKPN2242_05445
KPRKPR_4029
KPJN559_3812
KPID364_02740
KPAKPNJ1_04073
KPSKPNJ2_04095
KPXPMK1_02858(atsB)
KPBFH42_23615
KPNEKU54_019710
KPNULI86_19540
KPNKBN49_1575
KQUAVR78_11195
EAEEAE_13365
EARCCG31301
KARLGL98_18665
RORRORB6_12420
RAODSD31_18970
PGELG71_13730
IZHFEM41_07795
EBUCUC76_08800
SMARSM39_4951(atsB)
SMACSMDB11_4694(atsB)
SMWSMWW4_v1c05670
SMAFD781_0562
SERFL085_01230
SRZAXX16_4546
SERMCLM71_02720
SSURATE40_023550
SURIJ0X03_21115
SRHZFO014_07120
SENPKHA73_02605
SFOZ042_16765
PSIS70_17835
PSXDR96_2522
PSTABGK56_00150
PRGRB151_041290(atsB)
PVCG3341_13275
PMAGJI723_13190
 » show all
Reference
1  [PMID:10336424]
  Authors
Szameit C, Miech C, Balleininger M, Schmidt B, von Figura K, Dierks T
  Title
The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase.
  Journal
J Biol Chem 274:15375-81 (1999)
DOI:10.1074/jbc.274.22.15375
  Sequence
[kpn:KPN_00528]
Reference
2  [PMID:14749327]
  Authors
Fang Q, Peng J, Dierks T
  Title
Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB.
  Journal
J Biol Chem 279:14570-8 (2004)
DOI:10.1074/jbc.M313855200
Reference
3  [PMID:18558715]
  Authors
Grove TL, Lee KH, St Clair J, Krebs C, Booker SJ
  Title
In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme  that contains three [4Fe-4S] clusters.
  Journal
Biochemistry 47:7523-38 (2008)
DOI:10.1021/bi8004297
Other DBs
ExplorEnz - The Enzyme Database: 1.1.98.7
IUBMB Enzyme Nomenclature: 1.1.98.7
ExPASy - ENZYME nomenclature database: 1.1.98.7
BRENDA, the Enzyme Database: 1.1.98.7

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