KEGG ENZYME: 1.1.98.7

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

SENR:

STMDT2_30171

SEND:

DT104_31191

SENI:

CY43_16280

SEEN:

SE451236_21730

SPQ:	SPAB_03893

SEI:

SPC_3190

SEC:	SCH_3063(arsR)

SEH:	SeHA_C3365

SHB:

SU5_03621

SENH:

CFSAN002069_16535

SEEH:

SEEH1578_01740

SEE:	SNSL254_A3372

SENN:

SN31241_42470

SEW:	SeSA_A3298

SED:

SeD_A3467

SEG:

SG3017

SEL:

SPUL_3126

SEGA:

SPUCDC_3112

SET:

SEN2966

SENA:

AU38_15075

SENO:

AU37_15085

SENV:

AU39_15080

SENQ:

AU40_16995

SENL:

IY59_15685

SENJ:

CFSAN001992_17960

SEEB:

SEEB0189_004265

SEEP:

I137_14940

SENB:

BN855_31950

SENE:

IA1_15075

SES:	SARI_04508

SALZ:

EOS98_03705

KPN:

KPN_00528

KPU:

KP1_1454

KPM:	KPHS_13460

KPP:

A79E_3722

KPH:	KPNIH24_22060

KPZ:	KPNIH27_06265

KPV:	KPNIH29_06935

KPW:	KPNIH30_06945

KPY:	KPNIH31_06850

KPG:	KPNIH32_07050

KPC:	KPNIH10_06745

KPQ:	KPR0928_06660

KPT:	VK055_2015

KPO:	KPN2242_05445

KPR:

KPR_4029

KPJ:

N559_3812

KPI:	D364_02740

KPA:	KPNJ1_04073

KPS:	KPNJ2_04095

KPX:	PMK1_02858(atsB)

KPB:	FH42_23615

KPNE:

KU54_019710

KPNU:

LI86_19540

KPNK:

BN49_1575

KQU:	AVR78_11195

EAE:

EAE_13365

EAR:

CCG31301

KAR:	LGL98_18665

ROR:	RORB6_12420

RAO:	DSD31_18970

PGE:	LG71_13730

IZH:	FEM41_07795

EBU:	CUC76_08800

SMAR:

SM39_4951(atsB)

SMAC:

SMDB11_4694(atsB)

SMW:	SMWW4_v1c05670

SMAF:

D781_0562

SERF:

L085_01230

SRZ:	AXX16_4546

SERM:

CLM71_02720

SSUR:

ATE40_023550

SURI:

J0X03_21115

SRHZ:

FO014_07120

SENP:

KHA73_02605

SNEM:

NLX84_02750

SFO:	Z042_16765

PSI:

S70_17835

PSX:

DR96_2522

PSTA:

BGK56_00150

PTHA:

OI982_05520

PRG:	RB151_041290(atsB)

PVC:	G3341_13275

PMAG:

JI723_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

All links

Chemical substance (5)   
   KEGG COMPOUND (5)   
Chemical reaction (2)   
   KEGG REACTION (1)   
   KEGG RCLASS (1)   
Gene (102)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (94)   
   KEGG MGENES (7)   
Protein sequence (6)   
   UniProt (3)   
   SWISS-PROT (3)   
DNA sequence (10)   
   GenBank (5)   
   EMBL (5)   
Protein domain (6)   
   InterPro (6)   
All databases (131)   

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