KEGG   ENZYME: 1.12.5.1Help
Entry
EC 1.12.5.1                 Enzyme                                 

Name
hydrogen:quinone oxidoreductase;
hydrogen-ubiquinone oxidoreductase;
hydrogen:menaquinone oxidoreductase;
membrane-bound hydrogenase;
quinone-reactive Ni/Fe-hydrogenase
Class
Oxidoreductases;
Acting on hydrogen as donor;
With a quinone or similar compound as acceptor
BRITE hierarchy
Sysname
hydrogen:quinone oxidoreductase
Reaction(IUBMB)
H2 + menaquinone = menaquinol [RN:R02965]
Reaction(KEGG)
Substrate
H2 [CPD:C00282];
menaquinone [CPD:C00828]
Product
menaquinol [CPD:C05819]
Comment
Contains nickel, iron-sulfur clusters and cytochrome b. Also catalyses the reduction of water-soluble quinones (e.g. 2,3-dimethylnaphthoquinone) or viologen dyes (benzylviologen or methylviologen).
History
EC 1.12.5.1 created 1999 as EC 1.12.99.3, transferred 2002 to EC 1.12.5.1
Orthology
K05922  quinone-reactive Ni/Fe-hydrogenase large subunit
K05927  quinone-reactive Ni/Fe-hydrogenase small subunit
Genes
PDS: CAY62_05940 CAY62_05945
SON: SO_2098(hyaB) SO_2099(hyaA)
SFR: Sfri_2103 Sfri_2104
SAZ: Sama_1678 Sama_1679
SBL: Sbal_1888 Sbal_1889
SBM: Shew185_1914 Shew185_1915
SBN: Sbal195_1921 Sbal195_1922
SBP: Sbal223_2404 Sbal223_2405
SBT: Sbal678_1960 Sbal678_1961
SBS: Sbal117_2006 Sbal117_2007
HPJ: jhp_0574(hyaA) jhp_0575(hyaB)
HPG: HPG27_592(hydA) HPG27_593(hydB)
HPP: HPP12_0643(hydA) HPP12_0644(hydB)
HPB: HELPY_0739(hydB) HELPY_0740(hydA)
HPL: HPB8_831(hydA) HPB8_832(hydB)
HEF: HPF16_0728(hyaB) HPF16_0729(hyaA)
HPF: HPF30_0695(hyaB) HPF30_0696(hyaA)
HEQ: HPF32_0608(hyaA) HPF32_0609(hyaB)
HEX: HPF57_0655(hyaA) HPF57_0656(hyaB)
HPZ: HPKB_0711(hyaB) HPKB_0712(hyaA)
HPD: KHP_0688(hydB) KHP_0689(hyaA)
HPYO: HPOK113_0646(hyaA) HPOK113_0647(hyaB)
HPYL: HPOK310_0706(hyaB) HPOK310_0707(hyaA)
HHE: HH_0056(hyaA) HH_0057(hyaB) HH_0198
HAC: Hac_0744(hyaA) Hac_0745(hyaB)
HMS: HMU06120(hydA2) HMU09900(hydB) HMU09910(hydA)
HFE: HFELIS_12820(hydB) HFELIS_12830(hydA)
HCP: HCN_1167(hyaA) HCN_1168(hyaB) HCN_1570
WSU: WS1686 WS1687(HYDA)
CJE: Cj1266c(hydB) Cj1267c(hydA) Cj1399c(hydA2)
CJB: BN148_1266c(hydB) BN148_1267c(hydA) BN148_1399c(hydA2)
CJU: C8J_1210(hydB) C8J_1211(hydA) C8J_1313(hydA2)
CJI: CJSA_1205(hydB) CJSA_1206(hydA) CJSA_1330(hydA2)
CJM: CJM1_1247(hydB) CJM1_1248(hydA) CJM1_1356(hydA2)
CJS: CJS3_1311(hydB) CJS3_1312(hydA) CJS3_1494
CJY: QZ67_01345(hydB) QZ67_01346(hydA_2) QZ67_01533(hydA_3) QZ67_01534(hydA_4)
CJQ: UC78_1217(hydB) UC78_1218(hydA_1) UC78_1341(hydA_2)
CJR: CJE1402(hydB) CJE1403(hydA) CJE1586
CFT: CFF04554_0940(hydB) CFF04554_0941(hydA)
CFV: CFVI03293_0815(hydB)
CFX: CFV97608_1000(hydB)
CAMP: CFT03427_0932(hydB) CFT03427_0933(hydA)
CCV: CCV52592_1902(hydB) CCV52592_1903(hydA)
CCO: CCC13826_0100(hydB) CCC13826_0101(hydA)
CCOC: CCON33237_1010(hydB) CCON33237_1011(hydA)
CLA: Cla_0414(hydA) Cla_0712(hyaA) Cla_0713(hyaB)
CLL: CONCH_0417 CONCH_0724(hydA) CONCH_0725(hydB)
CCOF: VC76_02990(hydA_2) VC76_02995(hydB) VC76_07000(hydA_3)
CCOO: ATE51_00766(hydA_1) ATE51_02402(hydB) ATE51_02404(hydA_2)
CAJ: CIG1485E_0982(hydB) CIG1485E_0983(hydA)
CIS: CINS_0691(hydA) CINS_0692(hydB)
CVO: CVOL_0404 CVOL_0704(hydA) CVOL_0705(hydB)
CPEL: CPEL_0424 CPEL_0781(hydA) CPEL_0782(hydB)
CGRA: CGRAC_1164(hydB) CGRAC_1165(hydA)
CURE: CUREO_0784(hydA) CUREO_0785(hydB)
CHYO: CHH_0992(hydB) CHH_0993(hydA)
CSPF: CSF_1191(hydA) CSF_1192(hydB)
CCUN: CCUN_0543 CCUN_1375(hydB) CCUN_1376(hydA)
CLX: CLAN_1091(hydB) CLAN_1092(hydA)
CAVI: CAV_0707(hydA) CAV_0708(hydB) CAV_1139
ABU: Abu_1427(hydB) Abu_1428(hydA) Abu_1434(hyaB) Abu_1435(hyaA)
ABL: A7H1H_1448(hydB) A7H1H_1449(hydA) A7H1H_1453(hyaB) A7H1H_1454(hyaA)
SMUL: SMUL_1423(hydA) SMUL_1424(hydB)
 » show all
Taxonomy
Reference
1  [PMID:1587288]
  Authors
Dross F, Geisler V, Lenger R, Theis F, Krafft T, Fahrenholz F, Kojro E, Duchene A, Tripier D, Juvenal K, et al.
  Title
The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes.
  Journal
Eur J Biochem 206:93-102 (1992)
DOI:10.1111/j.1432-1033.1992.tb16905.x
  Sequence
Reference
2  [PMID:8319698]
  Authors
Dross F, Geisler V, Lenger R, Theis F, Krafft T, Fahrenholz F, Kojro E, Duchene A, Tripier D, Juvenal K, et al.
  Title
The quinone-reactive Ni/Fe-hydrogenase of Wolinella Succinogenes.
  Journal
Eur J Biochem 214:949-50 (1993)
DOI:10.1111/j.1432-1033.1993.tb17999.x
  Sequence
Reference
3  [PMID:9822828]
  Authors
Gross R, Simon J, Lancaster CR, Kroger A.
  Title
Identification of histidine residues in Wolinella succinogenes hydrogenase that are essential for menaquinone reduction by H2.
  Journal
Mol Microbiol 30:639-46 (1998)
DOI:10.1046/j.1365-2958.1998.01100.x
Reference
4  [PMID:9310376]
  Authors
Bernhard M, Benelli B, Hochkoeppler A, Zannoni D, Friedrich B.
  Title
Functional and structural role of the cytochrome b subunit of the membrane-bound hydrogenase complex of Alcaligenes eutrophus H16.
  Journal
Eur J Biochem 248:179-86 (1997)
DOI:10.1111/j.1432-1033.1997.00179.x
Reference
5  [PMID:8354459]
  Authors
Ferber DM, Maier RJ.
  Title
Hydrogen-ubiquinone oxidoreductase activity by the Bradyrhizobium japonicum membrane-bound hydrogenase.
  Journal
FEMS Microbiol Lett 110:257-64 (1993)
DOI:10.1111/j.1574-6968.1993.tb06331.x
Reference
6
  Authors
Ishii, M., Omori, T., Igarashi, Y., Adachi, O., Ameyama, M. and Kodama, T.
  Title
Methionaquinone is a direct natural electron-acceptor for the membrane-bound hydrogenase in Hydrogenobacter thermophilus strain TK-6.
  Journal
Agric Biol Chem 55:3011-3016 (1991)
Other DBs
ExplorEnz - The Enzyme Database: 1.12.5.1
IUBMB Enzyme Nomenclature: 1.12.5.1
ExPASy - ENZYME nomenclature database: 1.12.5.1
BRENDA, the Enzyme Database: 1.12.5.1
CAS: 151616-65-8

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