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
STM: STM3123
SEO: STM14_3772
SEV: STMMW_30831
SEY: SL1344_3097
SEM: STMDT12_C31760
SEJ: STMUK_3111
SEB: STM474_3272
SEF: UMN798_3393
SETU: STU288_15805
SETC: CFSAN001921_01410
SENI: CY43_16280
SEI: SPC_3190
SEC: SCH_3063(arsR)
SHB: SU5_03621
SED: SeD_A3467
SEG: SG3017
SEL: SPUL_3126
SET: SEN2966
SENA: AU38_15075
SENO: AU37_15085
SENV: AU39_15080
SENQ: AU40_16995
SENL: IY59_15685
SEEP: I137_14940
SENE: IA1_15075
KPN: KPN_00528
KPU: KP1_1454
KPP: A79E_3722
KPR: KPR_4029
KPJ: N559_3812
KPX: PMK1_02858(atsB)
KPNU: LI86_19540
KPNK: BN49_1575
EAE: EAE_13365
EAR: CCG31301
SMAR: SM39_4951(atsB)
SMAC: SMDB11_4694(atsB)
SMAF: D781_0562
SERF: L085_01230
PSI: S70_17835
PSX: DR96_2522
PRG: RB151_041290(atsB)
 » 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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