KEGG   ENZYME: 1.20.2.1
Entry
EC 1.20.2.1                 Enzyme                                 
Name
arsenate reductase (cytochrome c);
arsenite oxidase (ambiguous)
Class
Oxidoreductases;
Acting on phosphorus or arsenic in donors;
With a cytochrome as acceptor
Sysname
arsenite:cytochrome c oxidoreductase
Reaction(IUBMB)
arsenite + H2O + 2 oxidized cytochrome c = arsenate + 2 reduced cytochrome c + 2 H+ [RN:R09787]
Reaction(KEGG)
R09787
Substrate
arsenite [CPD:C06697];
H2O [CPD:C00001];
oxidized cytochrome c
Product
arsenate [CPD:C11215];
reduced cytochrome c [CPD:C00126];
H+ [CPD:C00080]
Comment
A molybdoprotein containing iron-sulfur clusters. Isolated from alpha-proteobacteria. Unlike EC 1.20.9.1, arsenate reductase (azurin), it does not use azurin as acceptor.
History
EC 1.20.2.1 created 2011
Orthology
K08355  arsenite oxidase small subunit
K08356  arsenite oxidase large subunit
Genes
VSPVS_II0658 VS_II0659
VTAA0943 A0944 B1225 B1226
VSLLTQ54_20390 LTQ54_20395
VSYK08M4_35820(aioB) K08M4_35830(aioA_1)
MBSMRBBS_1242(aoxB) MRBBS_1243(aoxA)
MPQABA45_06345
MVSMVIS_1833(aoxA)
MYAMORIYA_1165 MORIYA_1166
AEHMlg_1558
SHAILMH63_04690 LMH63_04695
GAIIMCC3135_25220
EPSL0Y14_10895 L0Y14_10900
HSIBOX17_13460 BOX17_13465
RSLRPSI07_mp0919(aoxA) RPSI07_mp0920(aoxB)
RSGJK151_18780 JK151_18785
CUHBJN34_21510 BJN34_21515
CBWRR42_s1794 RR42_s1795
CCUPBKK81_17850 BKK81_17855 BKK81_22395
CUUBKK79_24695 BKK79_24700
CUKKB879_31230 KB879_31235
BOCBG90_1022 BG90_1023
BVEAK36_5595 AK36_5596
BMJBMULJ_05810(asoA) BMULJ_05811(asoB) BMULJ_05832(asoB) BMULJ_05833(asoA)
BMUBmul_5678 Bmul_5679 Bmul_5703 Bmul_5704
BMKDM80_6068 DM80_6069 DM80_6143 DM80_6144
BURKDM992_39955 DM992_39960
PARBCJU94_00385 CJU94_00390
PGISI6I06_12610 I6I06_12615
PDIOPDMSB3_0039.2(aioB) PDMSB3_0040.2(aioA)
PPNODA70_08845 DA70_08850
CABASBC2_73790(aioB) SBC2_73800(aioA)
TVLFAZ95_24930 FAZ95_24935
AXXERS451415_05769(aioB) ERS451415_05770(aioA)
ADYHLG70_07540 HLG70_07545
RFRRfer_3084 Rfer_3085
OTKC6570_08745 C6570_08750
HPSEHPF_13640(aioB)
HYNF9K07_29420 F9K07_29425
HTNKI616_13715 KI616_13720
DRGH9K76_03270 H9K76_03275
HARHEAR0478(aoxB) HEAR0479(aoxA)
HEEhmeg3_02275 hmeg3_02280
TINTint_3061 Tint_3062
THITHI_3162(aoxB) THI_3163(aoxA)
METRBSY238_2675
SULFCAP31_08915 CAP31_08920
SPLBSFPGR_23330(soxF)
URUDSM104443_02691
UPLDSM104440_02414
AZDCDA09_11970 CDA09_11975
ATWC0099_09795 C0099_09800
BEBABWI17_13330
MOHIHQ72_14000 IHQ72_14005
AAKAA2016_4246 AA2016_4247
AMIHCO731_03145(aioB) CO731_03146(aioA)
AMISAmn_21870 Amn_21880
SAMESAMCFNEI73_pC1772(aioB) SAMCFNEI73_pC1773(aioA)
EAKEKH55_4985 EKH55_4986
RHTNT26_p10029(aioB) NT26_p10030(aioA)
BSEIKMZ68_21350 KMZ68_21355
BPAHQA639_35220
BRAZLRP30_02820 LRP30_02825
NHANham_4426 Nham_4427
PCAXAFIC_003115 AFIC_003116
BOFFQV39_32090 FQV39_32095
XAUXaut_3949 Xaut_3950
SNOSnov_1288 Snov_1289
ANCGBB76_17085 GBB76_17090
MOCBB934_26195 BB934_26200
CHELAL346_18905 AL346_18910
CDQBOQ54_03350 BOQ54_03355
BLAGBLTE_10210 BLTE_10220
MSCBN69_1400(aoxB) BN69_1401
MROSEHO51_05095 EHO51_05100
AUZSa4125_32580 Sa4125_32590
JAVOXU80_17520 OXU80_17525
NOHG5V57_02085 G5V57_02090
PSFPSE_5043 PSE_5044
LABPFJ695_09860 FJ695_09865
ACUTMRB58_23145 MRB58_23150
CSECseg_2507 Cseg_2508
RLIRLO149_c022030(aoxA) RLO149_c022040(aoxB)
CONTQ29_15470 TQ29_15475
SPSESULPSESMR1_00155(aioA) SULPSESMR1_00156(aioB)
AHTANTHELSMS3_01774(aioA) ANTHELSMS3_01775(aioB)
THAACFI11_15005 CFI11_15010
TGLHFZ77_15760 HFZ77_15765
HATRC74_20735
PSEWJHW44_16040 JHW44_16045
PSAPJHX88_09005 JHX88_09010
DAAAKL17_1594 AKL17_1595
PPSOQPJ95_16145 QPJ95_16150
PAMOBAR1_01585 BAR1_01590
PGVSL003B_2333 SL003B_2334
NSMJO391_20400 JO391_20405
AMVACMV_26640 ACMV_26650 ACMV_P2_00160 ACMV_P2_00170
SKUSulku_1032
SULRB649_04295
SBASulba_2413 Sulba_2414
SMULSMUL_3119(aioB) SMUL_3120(aioA)
SHALSHALO_2876 SHALO_2877
SULSSdiek1_1026 Sdiek1_1028
NISNIS_0033
BACIB1NLA3E_03580
GSTHW35_13485
BACQDOE78_14710
BACAFAY30_05805
BCOBcell_2932
BCOHBC6307_03535
BONA361_18050
CGOTJ1899_13040
CFIRNAF01_16185
CSOALIS82_03630 LIS82_16610
CSPGLS684_09815
VIRX953_02020
VHLBME96_01380
FECQNH15_19550
BSJUP17_09935
PBUTDTO10_23785
PPSRI6J18_11655
PFRIL8956_11020
POFGS400_18185
NMKCHR53_05940
NDTL1999_04460
NCMQNK12_03900
NNVQNH39_06015
MEKUHUW50_24820
AIAAWH56_015545
DOMRRU94_00135
EATEAT1b_1905
BBEBBR47_47180
BLRBRLA_c027090
BFMBP422_19300
BRWGOP56_06075
PMSKNP414_01413
PMQPM3016_1730
PMWB2K_08810
ACURJZ785_04745 JZ785_04750
CAUCaur_1209 Caur_1210
CHLChy400_1322 Chy400_1323
CAGCagg_0377 Cagg_0378
TTRTter_2537
DGEDgeo_1251
DDRDeide_08260
DMRDeima_1145
DPTDeipr_0889
DPDDeipe_0804
DSWQR90_01820
DCHSY84_03750
DABAUC44_05220
DPUSU48_09115
DFCDFI_03960
DEINDAAJ005_03325
DGADEGR_20740
TRATrad_0410
TTJTTHB127(TTHB127) TTHB128(TTHB128)
TTSThthe16_2239 Ththe16_2240
TSCTSC_c14680(aoxB) TSC_c14700(aoxA)
TAQTO73_0834 TO73_0835
TBCA0O31_02546 A0O31_02547
TANTKNN15_12350 KNN15_12355
MRBMrub_2869
MREK649_08180
PNDPla175_21920(aioB)
SUSAcid_2926
PFERIRI77_14250
ABACLuPra_00131(aioB)
CPBCphamn1_2364 Cphamn1_2365
CLIClim_0382 Clim_0383
HHOHydHO_0313 HydHO_0314
HYSHydSN_0324 HydSN_0325
TRDTHERU_04625 THERU_04630
NDENIDE3704(aoxA) NIDE3705(aoxB)
HALBEKH57_17170 EKH57_17175
HLCCHINAEXTREME13385 CHINAEXTREME13390
APEAPE_2556.1 APE_2563
ACJACAM_1597 ACAM_1598
STOSTK_23910 STK_23920
SOHD1869_13100 D1869_13105
SULABFU36_12340 BFU36_12370
SULLEWF20_14140 EWF20_14145
MCNMcup_1604 Mcup_1611
MHKDFR87_05070 DFR87_05105
MTENGWK48_00020 GWK48_11320
MJNMjAS7_1216 MjAS7_1224
AHOAhos_1882 Ahos_1883
AMANB6F84_04000 B6F84_04010
ABRIDFR85_00200 DFR85_00205 DFR85_00260
ASULDFR86_03900 DFR86_03910
ACIHHS5_06700 HS5_06710
CSTYKN1_02360 KN1_02370
STEPIC006_2112 IC006_2120
SMETRQ359_002115 RQ359_002123
PCLPcal_1369 Pcal_1370
PYRP186_1845 P186_1846
POGPogu_0531 Pogu_0532
 » show all
Reference
1  [PMID:15178476]
  Authors
vanden Hoven RN, Santini JM
  Title
Arsenite oxidation by the heterotroph Hydrogenophaga sp. str. NT-14: the arsenite oxidase and its physiological electron acceptor.
  Journal
Biochim Biophys Acta 1656:148-55 (2004)
DOI:10.1016/j.bbabio.2004.03.001
Reference
2  [PMID:17306216]
  Authors
Santini JM, Kappler U, Ward SA, Honeychurch MJ, vanden Hoven RN, Bernhardt PV
  Title
The NT-26 cytochrome c552 and its role in arsenite oxidation.
  Journal
Biochim Biophys Acta 1767:189-96 (2007)
DOI:10.1016/j.bbabio.2007.01.009
Reference
3  [PMID:19525272]
  Authors
Branco R, Francisco R, Chung AP, Morais PV
  Title
Identification of an aox system that requires cytochrome c in the highly arsenic-resistant bacterium Ochrobactrum tritici SCII24.
  Journal
Appl Environ Microbiol 75:5141-7 (2009)
DOI:10.1128/AEM.02798-08
  Sequence
Reference
4  [PMID:20421652]
  Authors
Lieutaud A, van Lis R, Duval S, Capowiez L, Muller D, Lebrun R, Lignon S, Fardeau ML, Lett MC, Nitschke W, Schoepp-Cothenet B
  Title
Arsenite oxidase from Ralstonia sp. 22: characterization of the enzyme and its interaction with soluble cytochromes.
  Journal
J Biol Chem 285:20433-41 (2010)
DOI:10.1074/jbc.M110.113761
Other DBs
ExplorEnz - The Enzyme Database: 1.20.2.1
IUBMB Enzyme Nomenclature: 1.20.2.1
ExPASy - ENZYME nomenclature database: 1.20.2.1
BRENDA, the Enzyme Database: 1.20.2.1

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