KEGG   ENZYME: 1.13.11.53Help
Entry
EC 1.13.11.53               Enzyme                                 

Name acireductone dioxygenase (Ni2+-requiring);
ARD;
2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase (ambiguous);
acireductone dioxygenase (ambiguous);
E-2
Class Oxidoreductases;
Acting on single donors with O2 as oxidant and incorporation of
oxygen into the substrate (oxygenases). The oxygen incorporated need
not be derived from O2;
With incorporation of two atoms of oxygen
BRITE hierarchy
Sysname 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one:oxygen oxidoreductase
(formate- and CO-forming)
Reaction(IUBMB) 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 =
3-(methylthio)propanoate + formate + CO [RN:R07363]
Reaction(KEGG) R07363
Show
Substrate 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one [CPD:C15606];
O2 [CPD:C00007]
Product 3-(methylthio)propanoate;
formate [CPD:C00058];
CO [CPD:C00237]
Comment Requires Ni2+. If iron(II) is bound instead of Ni2+, the reaction
catalysed by EC 1.13.11.54, acireductone dioxygenase
[iron(II)-requiring], occurs instead [1]. The enzyme from the
bacterium Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC
strain 8724 is involved in the methionine salvage pathway.
Pathway PATH: ec00270  Cysteine and methionine metabolism
PATH: ec01100  Metabolic pathways
Orthology KO: K08967  1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase
Genes HSA: 55256(ADI1)
PTR: 743384(ADI1)
MCC: 722050
MMU: 104923(Adi1)
RNO: 298934(Adi1)
CFA: 608836(ADI1)
BTA: 615764(ADI1)
ECB: 100072837
MDO: 100030804
OAA: 100092733 100092993
GGA: 421918(RCJMB04_7o8)
TGU: 100229689
XLA: 734860(adi1)
XTR: 448325(adi1)
DRE: 324079(adi1)
BFO: BRAFLDRAFT_119977
CIN: 100183249
SPU: 584367
DME: Dmel_CG32068
DPO: Dpse_GA16655
DAN: Dana_GF10605
DER: Dere_GG15448
DPE: Dper_GL16350
DSE: Dsec_GM25222
DSI: Dsim_GD14255
DYA: Dyak_GE21758
DGR: Dgri_GH15903
DMO: Dmoj_GI16556
AGA: AgaP_AGAP005618
AAG: AaeL_AAEL004860
CQU: CpipJ_CPIJ019272
AME: 551839
NVI: 100122447
TCA: 658827
API: 100161243(Acypi002479)
ISC: IscW_ISCW007295
CEL: F42F12.4
CBR: CBG00142
HMG: 100208060
ATH: AT4G14710(ATARD2) AT4G14716(ATARD1)
POP: POPTR_720244 POPTR_720930
RCU: RCOM_0911070
OSA: 4331707(Os03g0161800)
ZMA: 100285340
PPP: PHYPADRAFT_128349 PHYPADRAFT_134384 PHYPADRAFT_164159
CRE: CHLREDRAFT_137265(ARD1)
CME: CMQ369C
SCE: YMR009W(ADI1)
AGO: AGOS_ADR021W
KLA: KLLA0D14487g
LTH: KLTH0F12408g
DHA: DEHA0B15697g
PIC: PICST_37619
PPA: PAS_chr2-1_0422
VPO: Kpol_370p2
LEL: LELG_00784
ZRO: ZYRO0G01276g
CAL: CaO19.2306
CTP: CTRG_04094
CDU: CD36_10410
CGR: CAGL0K08800g
YLI: YALI0A14498g
SPO: SPBC887.01
NCR: NCU00147
PAN: PODANSg5271
MGR: MGG_06443
FGR: FG02600.1
ANI: AN6576.2
AFM: AFUA_6G04430
AOR: AO090701000107
ANG: An15g00990
AFV: AFLA_055600
PCS: Pc20g12170
NFI: NFIA_050970
CIM: CIMG_02680
URE: UREG_03084
SSL: SS1G_00301
BFU: BC1G_00847
CNE: CNH03570
CNB: CNBI3200
LBC: LACBIDRAFT_294466
MPR: MPER_05095
MBR: MONBRDRAFT_12562
DDI: DDB_0230998
TET: TTHERM_00467500
TBR: Tb927.4.360
TCR: 507873.60
LMA: LmjF20.0970
LIF: LinJ20.0990 LinJ34.3990
LBZ: LbrM20_V2.4060
PTI: PHATRDRAFT_25000
TPS: THAPSDRAFT_37443
YPG: YpAngola_A3329
YPP: YPDSF_2880
YPS: YPTB0876
YPI: YpsIP31758_3180
YPY: YPK_3319
YPB: YPTS_0917
YEN: YE3231(mntD)
ECA: ECA2986 ECA3485
PCT: PC1_2725 PC1_3301
PWA: Pecwa_1549 Pecwa_3455
ETA: ETA_26070
SGL: SG0273
ENT: Ent638_1141
ESA: ESA_02726
CTU: Ctu_12360(mtnD)
KPN: KPN_00643
KPE: KPK_3931(mtnD)
KPU: KP1_1594(mtnD)
CKO: CKO_03973
SPE: Spro_0944
DDA: Dd703_0920
DDC: Dd586_3256
DZE: Dd1591_0887
XFA: XF2210
XFT: PD1259
XFM: Xfasm12_1411
XFN: XfasM23_1344
XCC: XCC1819
XCB: XC_2370
XCA: xccb100_2106
XCV: XCV1885
XAC: XAC1839
XOO: XOO2138
XOM: XOO_2007
XOP: PXO_00847
SML: Smlt2188
SMT: Smal_1781
PAE: PA1684
PAU: PA14_42730
PAP: PSPA7_3588
PAG: PLES_36431
PPU: PP_1832
PPF: Pput_3878
PPG: PputGB1_1410
PPW: PputW619_1440
PST: PSPTO_2046
PSB: Psyr_1856
PSP: PSPPH_1815
PFL: PFL_4346
PFO: Pfl01_1725
PFS: PFLU4336
PEN: PSEEN1531
PMY: Pmen_1884
PSA: PST_2431
AVN: Avin_23790
MAQ: Maqu_0908
MCA: MCA0798
TGR: Tgr7_2624
HCH: HCH_01845
ABO: ABO_1446
AFE: Lferr_0595
AFR: AFE_0433
DAC: Daci_3175
SCL: sce1550 sce8993
HOH: Hoch_4249
PLA: Plav_1853
BBT: BBta_2511
RPA: RPA2352
RPT: Rpal_2596
GOX: GOX1243
GBE: GbCGDNIH1_2266
ACR: Acry_0018
GDI: GDI_0586(mtnD)
GDJ: Gdia_1414
APT: APA01_07350
BSU: BSU13620(mtnD)
BAN: BA4258
BAR: GBAA4258
BAA: BA_4717
BAT: BAS3949
BAH: BAMEG_4299
BAI: BAA_4281
BCE: BC4039
BCA: BCE_4106
BCZ: BCZK3796
BCR: BCAH187_A4170
BCB: BCB4264_A4148
BCU: BCAH820_4060
BCG: BCG9842_B1090
BCQ: BCQ_3829
BCX: BCA_4152
BCY: Bcer98_2738
BTK: BT9727_3781
BTL: BALH_3656
BWE: BcerKBAB4_3868
BLI: BL03542(mtnZ)
BLD: BLi01517(ykrZ)
BAY: RBAM_013400(mtnD)
BPU: BPUM_1255(mtnZ)
GKA: GK0956
GTN: GTNG_0844
GWC: GWCH70_0853
GYM: GYMC10_2371
GYC: GYMC61_1748
AFL: Aflv_1994
ESI: Exig_0427
EAT: EAT1b_1439
BBE: BBR47_48930(mtnD)
PJD: Pjdr2_2626
AAC: Aaci_0094
NFA: nfa14460
SMA: SAV_6661
FAL: FRAAL1410
SEN: SACE_3605
AMI: Amir_0987
LIL: LB293
LIC: LIC20227(ard)
LBJ: LBJ_4219
LBL: LBL_4233
LBI: LEPBI_I1308
LBF: LBF_1254
SYW: SYNW0652
SYC: syc0916_c
SYF: Synpcc7942_0608
SYD: Syncc9605_2021
SYE: Syncc9902_0651
SYG: sync_0589
SYR: SynRCC307_0459
SYX: SynWH7803_0560
SYP: SYNPCC7002_A0553
MAR: MAE_46350
CYP: PCC8801_1146
CYC: PCC7424_4156
CYH: Cyan8802_1176
ANA: all2724
NPU: Npun_R2028
AVA: Ava_4291
PMT: PMT0197
PMF: P9303_21601
TER: Tery_2668
AAE: aq_1975
HYA: HY04AAS1_1513
SUL: SYO3AOP1_1265
SAF: SULAZ_1232
PMX: PERMA_1873
Taxonomy
Reference
  Authors
  Title
  Journal
  Organism
1  [PMID:8407993]
Wray JW, Abeles RH.
A bacterial enzyme that catalyzes formation of carbon monoxide.
J. Biol. Chem. 268 (1993) 21466-9.
Klebsiella pneumoniae [GN:kpn]
Reference
  Authors
  Title


  Journal
  Organism
2  [PMID:7852397]
Wray JW, Abeles RH.
The methionine salvage pathway in Klebsiella pneumoniae and rat
liver. Identification and characterization of two novel
dioxygenases.
J. Biol. Chem. 270 (1995) 3147-53.
Rattus norvegicus [GN:rno], Klebsiella pneumoniae [GN:kpn]
Reference
  Authors
  Title

  Journal
  Organism
3  [PMID:2838472]
Furfine ES, Abeles RH.
Intermediates in the conversion of 5'-S-methylthioadenosine to
methionine in Klebsiella pneumoniae.
J. Biol. Chem. 263 (1988) 9598-606.
Klebsiella pneumoniae [GN:kpn]
Reference
  Authors
  Title
  Journal
  Organism
4  [PMID:9880484]
Dai Y, Wensink PC, Abeles RH.
One protein, two enzymes.
J. Biol. Chem. 274 (1999) 1193-5.
Klebsiella pneumoniae [GN:kpn]
Reference
  Authors
  Title

  Journal
  Organism
5  [PMID:10481280]
Mo H, Dai Y, Pochapsky SS, Pochapsky TC.
1H, 13C and 15N NMR assignments for a carbon monoxide generating
metalloenzyme from Klebsiella pneumoniae.
J. Biomol. NMR. 14 (1999) 287-8.
Klebsiella pneumoniae [GN:kpn]
Reference
  Authors
  Title

  Journal
  Organism
6  [PMID:11371200]
Dai Y, Pochapsky TC, Abeles RH.
Mechanistic studies of two dioxygenases in the methionine salvage
pathway of Klebsiella pneumoniae.
Biochemistry. 40 (2001) 6379-87.
Klebsiella pneumoniae [GN:kpn]
Reference
  Authors
  Title

  Journal
  Organism
7  [PMID:12022880]
Al-Mjeni F, Ju T, Pochapsky TC, Maroney MJ.
XAS investigation of the structure and function of Ni in
acireductone dioxygenase.
Biochemistry. 41 (2002) 6761-9.
Klebsiella pneumoniae [GN:kpn]
Reference
  Authors
  Title

  Journal
  Organism
8  [PMID:12402029]
Pochapsky TC, Pochapsky SS, Ju T, Mo H, Al-Mjeni F, Maroney MJ.
Modeling and experiment yields the structure of acireductone
dioxygenase from Klebsiella pneumoniae.
Nat. Struct. Biol. 9 (2002) 966-72.
Klebsiella pneumoniae [GN:kpn]
Other DBs ExplorEnz - The Enzyme Database: 1.13.11.53
IUBMB Enzyme Nomenclature: 1.13.11.53
ExPASy - ENZYME nomenclature database: 1.13.11.53
BRENDA, the Enzyme Database: 1.13.11.53

KEGG   ENZYME: 1.13.11.54Help
Entry
EC 1.13.11.54               Enzyme                                 

Name acireductone dioxygenase [iron(II)-requiring];
ARD';
2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase (ambiguous);
acireductone dioxygenase (ambiguous);
E-2';
E-3 dioxygenase
Class Oxidoreductases;
Acting on single donors with O2 as oxidant and incorporation of
oxygen into the substrate (oxygenases). The oxygen incorporated need
not be derived from O2;
With incorporation of two atoms of oxygen
BRITE hierarchy
Sysname 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one:oxygen oxidoreductase
(formate-forming)
Reaction(IUBMB) 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 =
4-(methylthio)-2-oxobutanoate + formate [RN:R07364]
Reaction(KEGG) R07364
Show
Substrate 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one [CPD:C15606];
O2 [CPD:C00007]
Product 4-methylthio-2-oxobutanoate [CPD:C01180];
formate [CPD:C00058]
Comment Requires iron(II). If Ni2+ is bound instead of iron(II), the
reaction catalysed by EC 1.13.11.53, acireductone dioxygenase
(Ni2+-requiring), occurs instead. The enzyme from the bacterium
Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC strain 8724
is involved in the methionine salvage pathway.
Pathway PATH: ec00270  Cysteine and methionine metabolism
Orthology KO: K08967  1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase
Genes HSA: 55256(ADI1)
PTR: 743384(ADI1)
MCC: 722050
MMU: 104923(Adi1)
RNO: 298934(Adi1)
CFA: 608836(ADI1)
BTA: 615764(ADI1)
ECB: 100072837
MDO: 100030804
OAA: 100092733 100092993
GGA: 421918(RCJMB04_7o8)
TGU: 100229689
XLA: 734860(adi1)
XTR: 448325(adi1)
DRE: 324079(adi1)
BFO: BRAFLDRAFT_119977
CIN: 100183249
SPU: 584367
DME: Dmel_CG32068
DPO: Dpse_GA16655
DAN: Dana_GF10605
DER: Dere_GG15448
DPE: Dper_GL16350
DSE: Dsec_GM25222
DSI: Dsim_GD14255
DYA: Dyak_GE21758
DGR: Dgri_GH15903
DMO: Dmoj_GI16556
AGA: AgaP_AGAP005618
AAG: AaeL_AAEL004860
CQU: CpipJ_CPIJ019272
AME: 551839
NVI: 100122447
TCA: 658827
API: 100161243(Acypi002479)
ISC: IscW_ISCW007295
CEL: F42F12.4
CBR: CBG00142
HMG: 100208060
ATH: AT4G14710(ATARD2) AT4G14716(ATARD1)
POP: POPTR_720244 POPTR_720930
RCU: RCOM_0911070
OSA: 4331707(Os03g0161800)
ZMA: 100285340
PPP: PHYPADRAFT_128349 PHYPADRAFT_134384 PHYPADRAFT_164159
CRE: CHLREDRAFT_137265(ARD1)
CME: CMQ369C
SCE: YMR009W(ADI1)
AGO: AGOS_ADR021W
KLA: KLLA0D14487g
LTH: KLTH0F12408g
DHA: DEHA0B15697g
PIC: PICST_37619
PPA: PAS_chr2-1_0422
VPO: Kpol_370p2
LEL: LELG_00784
ZRO: ZYRO0G01276g
CAL: CaO19.2306
CTP: CTRG_04094
CDU: CD36_10410
CGR: CAGL0K08800g
YLI: YALI0A14498g
SPO: SPBC887.01
NCR: NCU00147
PAN: PODANSg5271
MGR: MGG_06443
FGR: FG02600.1
ANI: AN6576.2
AFM: AFUA_6G04430
AOR: AO090701000107
ANG: An15g00990
AFV: AFLA_055600
PCS: Pc20g12170
NFI: NFIA_050970
CIM: CIMG_02680
URE: UREG_03084
SSL: SS1G_00301
BFU: BC1G_00847
CNE: CNH03570
CNB: CNBI3200
LBC: LACBIDRAFT_294466
MPR: MPER_05095
MBR: MONBRDRAFT_12562
DDI: DDB_0230998
TET: TTHERM_00467500
TBR: Tb927.4.360
TCR: 507873.60
LMA: LmjF20.0970
LIF: LinJ20.0990 LinJ34.3990
LBZ: LbrM20_V2.4060
PTI: PHATRDRAFT_25000
TPS: THAPSDRAFT_37443
YPG: YpAngola_A3329
YPP: YPDSF_2880
YPS: YPTB0876
YPI: YpsIP31758_3180
YPY: YPK_3319
YPB: YPTS_0917
YEN: YE3231(mntD)
ECA: ECA2986 ECA3485
PCT: PC1_2725 PC1_3301
PWA: Pecwa_1549 Pecwa_3455
ETA: ETA_26070
SGL: SG0273
ENT: Ent638_1141
ESA: ESA_02726
CTU: Ctu_12360(mtnD)
KPN: KPN_00643
KPE: KPK_3931(mtnD)
KPU: KP1_1594(mtnD)
CKO: CKO_03973
SPE: Spro_0944
DDA: Dd703_0920
DDC: Dd586_3256
DZE: Dd1591_0887
XFA: XF2210
XFT: PD1259
XFM: Xfasm12_1411
XFN: XfasM23_1344
XCC: XCC1819
XCB: XC_2370
XCA: xccb100_2106
XCV: XCV1885
XAC: XAC1839
XOO: XOO2138
XOM: XOO_2007
XOP: PXO_00847
SML: Smlt2188
SMT: Smal_1781
PAE: PA1684
PAU: PA14_42730
PAP: PSPA7_3588
PAG: PLES_36431
PPU: PP_1832
PPF: Pput_3878
PPG: PputGB1_1410
PPW: PputW619_1440
PST: PSPTO_2046
PSB: Psyr_1856
PSP: PSPPH_1815
PFL: PFL_4346
PFO: Pfl01_1725
PFS: PFLU4336
PEN: PSEEN1531
PMY: Pmen_1884
PSA: PST_2431
AVN: Avin_23790
MAQ: Maqu_0908
MCA: MCA0798
TGR: Tgr7_2624
HCH: HCH_01845
ABO: ABO_1446
AFE: Lferr_0595
AFR: AFE_0433
DAC: Daci_3175
SCL: sce1550 sce8993
HOH: Hoch_4249
PLA: Plav_1853
BBT: BBta_2511
RPA: RPA2352
RPT: Rpal_2596
GOX: GOX1243
GBE: GbCGDNIH1_2266
ACR: Acry_0018
GDI: GDI_0586(mtnD)
GDJ: Gdia_1414
APT: APA01_07350
BSU: BSU13620(mtnD)
BAN: BA4258
BAR: GBAA4258
BAA: BA_4717
BAT: BAS3949
BAH: BAMEG_4299
BAI: BAA_4281
BCE: BC4039
BCA: BCE_4106
BCZ: BCZK3796
BCR: BCAH187_A4170
BCB: BCB4264_A4148
BCU: BCAH820_4060
BCG: BCG9842_B1090
BCQ: BCQ_3829
BCX: BCA_4152
BCY: Bcer98_2738
BTK: BT9727_3781
BTL: BALH_3656
BWE: BcerKBAB4_3868
BLI: BL03542(mtnZ)
BLD: BLi01517(ykrZ)
BAY: RBAM_013400(mtnD)
BPU: BPUM_1255(mtnZ)
GKA: GK0956
GTN: GTNG_0844
GWC: GWCH70_0853
GYM: GYMC10_2371
GYC: GYMC61_1748
AFL: Aflv_1994
ESI: Exig_0427
EAT: EAT1b_1439
BBE: BBR47_48930(mtnD)
PJD: Pjdr2_2626
AAC: Aaci_0094
NFA: nfa14460
SMA: SAV_6661
FAL: FRAAL1410
SEN: SACE_3605
AMI: Amir_0987
LIL: LB293
LIC: LIC20227(ard)
LBJ: LBJ_4219
LBL: LBL_4233
LBI: LEPBI_I1308
LBF: LBF_1254
SYW: SYNW0652
SYC: syc0916_c
SYF: Synpcc7942_0608
SYD: Syncc9605_2021
SYE: Syncc9902_0651
SYG: sync_0589
SYR: SynRCC307_0459
SYX: SynWH7803_0560
SYP: SYNPCC7002_A0553
MAR: MAE_46350
CYP: PCC8801_1146
CYC: PCC7424_4156
CYH: Cyan8802_1176
ANA: all2724
NPU: Npun_R2028
AVA: Ava_4291
PMT: PMT0197
PMF: P9303_21601
TER: Tery_2668
AAE: aq_1975
HYA: HY04AAS1_1513
SUL: SYO3AOP1_1265
SAF: SULAZ_1232
PMX: PERMA_1873
Taxonomy
Structures PDB: 2HJI  
Reference
  Authors
  Title
  Journal
  Organism
1  [PMID:8407993]
Wray JW, Abeles RH.
A bacterial enzyme that catalyzes formation of carbon monoxide.
J. Biol. Chem. 268 (1993) 21466-9.
Klebsiella pneumoniae [GN:kpn]
Reference
  Authors
  Title


  Journal
  Organism
2  [PMID:7852397]
Wray JW, Abeles RH.
The methionine salvage pathway in Klebsiella pneumoniae and rat
liver. Identification and characterization of two novel
dioxygenases.
J. Biol. Chem. 270 (1995) 3147-53.
Rattus norvegicus [GN:rno], Klebsiella pneumoniae [GN:kpn]
Reference
  Authors
  Title

  Journal
  Organism
3  [PMID:2838472]
Furfine ES, Abeles RH.
Intermediates in the conversion of 5'-S-methylthioadenosine to
methionine in Klebsiella pneumoniae.
J. Biol. Chem. 263 (1988) 9598-606.
Klebsiella pneumoniae [GN:kpn]
Reference
  Authors
  Title
  Journal
  Organism
4  [PMID:9880484]
Dai Y, Wensink PC, Abeles RH.
One protein, two enzymes.
J. Biol. Chem. 274 (1999) 1193-5.
Klebsiella pneumoniae [GN:kpn]
Reference
  Authors
  Title

  Journal
  Organism
5  [PMID:10481280]
Mo H, Dai Y, Pochapsky SS, Pochapsky TC.
1H, 13C and 15N NMR assignments for a carbon monoxide generating
metalloenzyme from Klebsiella pneumoniae.
J. Biomol. NMR. 14 (1999) 287-8.
Klebsiella pneumoniae [GN:kpn]
Reference
  Authors
  Title

  Journal
  Organism
6  [PMID:11371200]
Dai Y, Pochapsky TC, Abeles RH.
Mechanistic studies of two dioxygenases in the methionine salvage
pathway of Klebsiella pneumoniae.
Biochemistry. 40 (2001) 6379-87.
Klebsiella pneumoniae [GN:kpn]
Reference
  Authors
  Title

  Journal
  Organism
7  [PMID:12022880]
Al-Mjeni F, Ju T, Pochapsky TC, Maroney MJ.
XAS investigation of the structure and function of Ni in
acireductone dioxygenase.
Biochemistry. 41 (2002) 6761-9.
Klebsiella pneumoniae [GN:kpn]
Reference
  Authors
  Title

  Journal
  Organism
8  [PMID:12402029]
Pochapsky TC, Pochapsky SS, Ju T, Mo H, Al-Mjeni F, Maroney MJ.
Modeling and experiment yields the structure of acireductone
dioxygenase from Klebsiella pneumoniae.
Nat. Struct. Biol. 9 (2002) 966-72.
Klebsiella pneumoniae [GN:kpn]
Other DBs ExplorEnz - The Enzyme Database: 1.13.11.54
IUBMB Enzyme Nomenclature: 1.13.11.54
ExPASy - ENZYME nomenclature database: 1.13.11.54
BRENDA, the Enzyme Database: 1.13.11.54

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