KEGG   ENZYME: 1.97.1.9Help
Entry
EC 1.97.1.9                 Enzyme                                 

Name
selenate reductase
Class
Oxidoreductases;
Other oxidoreductases;
Sole sub-subclass for oxidoreductases that do not belong in the other subclasses
BRITE hierarchy
Sysname
selenite:reduced acceptor oxidoreductase
Reaction(IUBMB)
selenite + H2O + acceptor = selenate + reduced acceptor [RN:R07229]
Reaction(KEGG)
Substrate
selenite [CPD:C05684];
H2O [CPD:C00001];
acceptor [CPD:C00028]
Product
selenate [CPD:C05697];
reduced acceptor [CPD:C00030]
Comment
The periplasmic enzyme from Thauera selenatis is a complex comprising three heterologous subunits (alpha, beta and gamma) that contains molybdenum, iron, acid-labile sulfide and heme b as cofactor constituents. Nitrate, nitrite, chlorate and sulfate are not substrates. A number of compounds, including acetate, lactate, pyruvate, and certain sugars, amino acids, fatty acids, di- and tricarboxylic acids, and benzoate can serve as electron donors.
History
EC 1.97.1.9 created 2003
Pathway
ec00450  Selenocompound metabolism
Orthology
K07309  Tat-targeted selenate reductase subunit YnfE
K07310  Tat-targeted selenate reductase subunit YnfF
K12527  putative selenate reductase
Genes
ECO: b1587(ynfE) b1588(ynfF) b2878(ygfK)
ECJ: JW1579(ynfE) JW5260(ynfF) JW5923(ygfK)
ECD: ECDH10B_1720(ynfE) ECDH10B_1721(ynfF) ECDH10B_3053(ygfK)
EBW: BWG_1401(ynfE) BWG_1402(ynfF) BWG_2604(ygfK)
ECOK: ECMDS42_1257(ynfE) ECMDS42_1258(ynfF) ECMDS42_2378(ygfK)
ECE: Z2575 Z2576 Z4217
ECS: ECs2293 ECs2294 ECs3751
ECF: ECH74115_2296(ynfE) ECH74115_2297 ECH74115_4168
ETW: ECSP_2151(ynfE) ECSP_2152(ynfF) ECSP_3848(ygfK)
ELX: CDCO157_2130 CDCO157_2131 CDCO157_3504
EOJ: ECO26_2291(ynfF) ECO26_3967(ygfK)
EOI: ECO111_2056(ynfF) ECO111_3616(ygfK)
EOH: ECO103_1726(ynfE) ECO103_1727(ynfF) ECO103_3453(ygfK)
ECG: E2348C_1671(ynfE) E2348C_1672(ynfF)
EOK: G2583_1981(ynfE) G2583_1982(ynfF) G2583_3532(ygfK)
ECC: c1977(ynfE) c1978(ynfF) c3456(ygfK)
ECP: ECP_2872
ECI: UTI89_C1774(ynfE) UTI89_C1775(ynfF) UTI89_C3263(ygfK)
ECV: APECO1_3648(ygfK) APECO1_670(ynfE) APECO1_671(ynfF)
ECR: ECIAI1_1637(ynfE) ECIAI1_1638(ynfF) ECIAI1_2998(ygfK)
ECQ: ECED1_1757(ynfF) ECED1_3338(ygfK)
ECK: EC55989_1752(ynfE) EC55989_1753(ynfF) EC55989_3165(ygfK)
ECT: ECIAI39_1470(ynfF) ECIAI39_1471(ynfE) ECIAI39_3293(ygfK)
EOC: CE10_1857(ynfE) CE10_1858(ynfF) CE10_3317(ygfK)
EUM: ECUMN_1872(ynfE) ECUMN_1873(ynfF) ECUMN_3221(ygfK)
ECZ: ECS88_1632(ynfE) ECS88_1633(ynfF) ECS88_3157(ygfK)
EBR: ECB_01556(ynfE) ECB_01557(ynfF) ECB_02711(ygfK)
EKF: KO11_08375(ygfK) KO11_14815(ynfF) KO11_14820(ynfE)
EAB: ECABU_c17830(ynfE) ECABU_c17840(ynfF) ECABU_c31590(ygfK)
ENA: ECNA114_1632(ynfE) ECNA114_1633(ynfF1) ECNA114_1634(ynfF) ECNA114_2919(ygfK)
ELW: ECW_m1752(ynfE) ECW_m1753(ynfF) ECW_m3131(ygfK)
ELL: WFL_08580(ynfE) WFL_08585(ynfF) WFL_15290(ygfK)
ELC: i14_1800(ynfE) i14_1801(ynfF) i14_3175(ygfK)
ELD: i02_1800(ynfE) i02_1801(ynfF) i02_3175(ygfK)
EBL: ECD_01556(ynfE) ECD_01557(ynfF) ECD_02711(ygfK)
EBE: B21_01546(ynfE) B21_01547(ynfF) B21_02673(ygfK)
ELF: LF82_3172(ygfK) LF82_3571(ynfE)
ECOI: ECOPMV1_01682(dmsA_2) ECOPMV1_01683(dmsA_3) ECOPMV1_03150(gltD_2)
STY: STY1565(dmsA1) STY1566(dmsA2)
STT: t1419(dmsA) t1420(dmsA)
SEY: SL1344_1428(dmsA2) SL1344_1429(dmsA1)
SEB: STM474_1508(ynff) STM474_1509(ynfe)
SEF: UMN798_1561(dmsA2) UMN798_1562(dmsA1)
SENR: STMDT2_14251(dmsA2) STMDT2_14261(dmsA1)
SEND: DT104_14681(dmsA2) DT104_14691(dmsA1)
SPT: SPA1356
SEK: SSPA1261
SEI: SPC_2230(dmsA1) SPC_2231(dmsA2)
SEC: SCH_1515(ynfF) SCH_1516(ynfE)
SEG: SG1622(dmsA3)
SEL: SPUL_1314
SEGA: SPUCDC_1314 SPUCDC_1315(dmsA1)
SET: SEN1551(dmsA1) SEN1552(dmsA3)
SBG: SBG_1325(dmsA2) SBG_1326(dmsA1)
SFL: SF1607
SFV: SFV_1601
SFE: SFxv_1805(ynfF)
SFT: NCTC1_01733(dmsA_3) NCTC1_01745(dmsA_4) NCTC1_01746(ynfF)
SBO: SBO_1548
SBC: SbBS512_E1773(ynfE) SbBS512_E1774(arnT)
ENC: ECL_02189
ECLO: ENC_12140
EEC: EcWSU1_02007(ynfE)
ECLX: LI66_10050
ECLY: LI62_10835
CTU: CTU_22090(ynfE)
KPN: KPN_01580(ynfE)
KPU: KP1_2603(ynfE)
KPP: A79E_2656
KPT: VK055_0920(dmsA)
KPE: KPK_2875
KPR: KPR_2730
KPX: PMK1_03899(ynfE)
KPNU: LI86_13690
KPNK: BN49_2690
KVA: Kvar_2777
KOE: A225_3547
CRO: ROD_33961
SPE: Spro_1687
RAA: Q7S_07025
SOD: Sant_0571(dmsA1)
MMK: MU9_1064
ETR: ETAE_3169
ETD: ETAF_2860
ETE: ETEE_1398(ygfK)
ASU: Asuc_1524
PPR: PBPRA1943(C3456)
SHL: Shal_0648
AHA: AHA_2170
AVR: B565_1856
ASR: WL1483_683(ygfK)
DTR: RSDT_0735(ygfK)
DSF: UWK_01312
HOH: Hoch_2603
EFA: EF2581
EFL: EF62_2750
EFI: OG1RF_11961(ygfK)
EFS: EFS1_2059
EFN: DENG_02519(ygfK)
EFQ: DR75_1290(ygfK)
THL: TEH_06280
CBO: CBO2884
CBA: CLB_2848
CBH: CLC_2781
CBY: CLM_3280
CBL: CLK_2278
CBB: CLD_1658
CBI: CLJ_B3138
CBF: CLI_2940
CBE: Cbei_1973
CBZ: Cbs_1973
CBEI: LF65_02143
CLS: CXIVA_03990(GltD)
CSQ: CSCA_0234
CCT: CC1_06320
ROB: CK5_30740
RTO: RTO_24270
CPY: Cphy_1495
HMO: HM1_2651
ELM: ELI_2448
OVA: OBV_34930
MTA: Moth_1949
APR: Apre_1428
VPR: Vpar_1267
MED: MELS_0605
PUF: UFO1_1843
PFT: JBW_02534
ELE: Elen_0422
APV: Apar_0237
BHY: BHWA1_00069(gltD)
BRM: Bmur_2656
BPO: BP951000_0727(gltD)
BPW: WESB_2047(gltD)
BIP: Bint_1932(gltD)
TAI: Taci_0423
BLQ: L21SP5_02724(gltD_4)
CABY: Cabys_2131
BANA: BARAN1_0919(YgfK)
 » show all
Taxonomy
Reference
1  [PMID:9295321]
  Authors
Schroder I, Rech S, Krafft T, Macy JM.
  Title
Purification and characterization of the selenate reductase from Thauera selenatis.
  Journal
J Biol Chem 272:23765-8 (1997)
DOI:10.1074/jbc.272.38.23765
  Sequence
Reference
2  [PMID:8427805]
  Authors
Macy JM, Rech S, Auling G, Dorsch M, Stackebrandt E, Sly LI.
  Title
Thauera selenatis gen. nov., sp. nov., a member of the beta subclass of Proteobacteria with a novel type of anaerobic respiration.
  Journal
Int J Syst Bacteriol 43:135-42 (1993)
DOI:10.1099/00207713-43-1-135
Reference
3  [PMID:10826693]
  Authors
Krafft T, Bowen A, Theis F, Macy JM.
  Title
Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase of Thauera selenatis.
  Journal
DNA Seq 10:365-77 (2000)
  Sequence
Reference
4  [PMID:10525169]
  Authors
Stolz JF, Oremland RS.
  Title
Bacterial respiration of arsenic and selenium.
  Journal
FEMS Microbiol Rev 23:615-27 (1999)
DOI:10.1111/j.1574-6976.1999.tb00416.x
Other DBs
ExplorEnz - The Enzyme Database: 1.97.1.9
IUBMB Enzyme Nomenclature: 1.97.1.9
ExPASy - ENZYME nomenclature database: 1.97.1.9
BRENDA, the Enzyme Database: 1.97.1.9
CAS: 146359-71-9

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