KEGG   ENZYME: 1.1.5.5
Entry
EC 1.1.5.5                  Enzyme                                 

Name
alcohol dehydrogenase (quinone);
type III ADH;
membrane associated quinohaemoprotein alcohol dehydrogenase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With a quinone or similar compound as acceptor
Sysname
alcohol:quinone oxidoreductase
Reaction(IUBMB)
ethanol + ubiquinone = acetaldehyde + ubiquinol [RN:R09479]
Reaction(KEGG)
R09479
Substrate
ethanol [CPD:C00469];
ubiquinone [CPD:C00399]
Product
acetaldehyde [CPD:C00084];
ubiquinol [CPD:C00390]
Comment
Only described in acetic acid bacteria where it is involved in acetic acid production. Associated with membrane. Electron acceptor is membrane ubiquinone. A model structure suggests that, like all other quinoprotein alcohol dehydrogenases, the catalytic subunit has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ; the catalytic subunit also has a heme c in the C-terminal domain. The enzyme has two additional subunits, one of which contains three molecules of heme c. It does not require amines for activation. It has a restricted substrate specificity, oxidizing a few primary alcohols (C2 to C6), but not methanol, secondary alcohols and some aldehydes. It is assayed with phenazine methosulfate or with ferricyanide.
History
EC 1.1.5.5 created 2009, modified 2010
Pathway
ec00010  Glycolysis / Gluconeogenesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
ec01120  Microbial metabolism in diverse environments
Orthology
K22473  alcohol dehydrogenase (quinone), dehydrogenase subunit
K22474  alcohol dehydrogenase (quinone), cytochrome c subunit
Genes
KPU: KP1_3157
KPM: KPHS_30610
KPP: A79E_2173
KPH: KPNIH24_13130
KPZ: KPNIH27_14665
KPV: KPNIH29_15310
KPW: KPNIH30_15595
KPY: KPNIH31_14450
KPG: KPNIH32_15490
KPC: KPNIH10_15125
KPJ: N559_2209
KPNU: LI86_10985
KPNK: BN49_3187
KVA: Kvar_2193
KPE: KPK_2251
EAE: EAE_17480
EAR: CCG30395
EBF: D782_2835
PSTS: E05_00130
SPLY: Q5A_010800
SERF: L085_17940
RAA: Q7S_23806
EAM: EAMY_3265
EAY: EAM_0338
ETA: ETA_30590
EPY: EpC_32630
PAM: PANA_0302(adhB)
PAJ: PAJ_3463(adhB)
PVA: Pvag_3561
PSTW: DSJ_03270
PAEV: N297_2339
PAEI: N296_2339
PAEP: PA1S_14290
PAEM: U769_13875
PAEL: T223_15520
PAEG: AI22_19565
PAEC: M802_2336
PAEO: M801_2338
PPUN: PP4_22070 PP4_27710(gadA)
PFL: PFL_0055
PPRO: PPC_0059
PFS: PFLU_0053(adhB) PFLU_2270
PEN: PSEEN2170
PSES: PSCI_3416
PSEM: TO66_00270
PSOS: POS17_0059
AVL: AvCA_00910(gadh2)
AVD: AvCA6_00910(gadh2)
ACX: Achr_f920(gadh2)
PAR: Psyc_1440
PHA: PSHAa1829
NWE: SAMEA3174300_0545(adhB_1)
NZO: SAMEA4504057_1735(adhB_2)
NCI: NCTC10296_01014(adhB_1)
RME: Rmet_2502
BPSE: BDL_1283
BPSM: BBQ_2708
BPSU: BBN_2831
BPSD: BBX_3230
BPK: BBK_765(adhB)
BPSH: DR55_374
BPSA: BBU_1432
BUT: X994_1995
BMJ: BMULJ_04126(cccA)
BGU: KS03_2457
BGO: BM43_4681
BXB: DR64_6997
PPNO: DA70_07795
PPNM: LV28_22785
PPUL: RO07_17200
PSPU: NA29_19955
PAPI: SG18_15980
BAV: BAV1805(adhB) BAV3247
TEA: KUI_1449(adhB)
TEG: KUK_0751(adhB)
TAS: TASI_1428
TAT: KUM_1086(adhB)
AMIM: MIM_c15380(adhB)
OAN: Oant_0689
OAH: DR92_2252
HDI: HDIA_P0070(adhB_2)
SECH: B18_23405
GOY: GLS_c05020(adhB1) GLS_c11360(adhB3) GLS_c11370(adhA)
GDI: GDI0856 GDI2040(adhA) GDI2041(adhB)
KSC: CD178_00411(adhA) CD178_00412(adhB_1) CD178_01765(adhB_2)
APK: APA386B_1574(adhB) APA386B_1575(adhA)
ASZ: ASN_1383(adhA) ASN_1513(adhA) ASN_1514(adhB) ASN_2761 ASN_3435
 » show all
Reference
1  [PMID:18321602]
  Authors
Gomez-Manzo S, Contreras-Zentella M, Gonzalez-Valdez A, Sosa-Torres M, Arreguin-Espinoza R, Escamilla-Marvan E
  Title
The PQQ-alcohol dehydrogenase of Gluconacetobacter diazotrophicus.
  Journal
Int J Food Microbiol 125:71-8 (2008)
DOI:10.1016/j.ijfoodmicro.2007.10.015
Reference
2  [PMID:16636451]
  Authors
Shinagawa E, Toyama H, Matsushita K, Tuitemwong P, Theeragool G, Adachi O
  Title
A novel type of formaldehyde-oxidizing enzyme from the membrane of Acetobacter sp. SKU 14.
  Journal
Biosci Biotechnol Biochem 70:850-7 (2006)
DOI:10.1271/bbb.70.850
Reference
3  [PMID:16233574]
  Authors
Chinnawirotpisan P, Theeragool G, Limtong S, Toyama H, Adachi OO, Matsushita K
  Title
Quinoprotein alcohol dehydrogenase is involved in catabolic acetate production, while NAD-dependent alcohol dehydrogenase in ethanol assimilation in Acetobacter  pasteurianus SKU1108.
  Journal
J Biosci Bioeng 96:564-71 (2003)
DOI:10.1016/S1389-1723(04)70150-4
Reference
4  [PMID:9526036]
  Authors
Frebortova J, Matsushita K, Arata H, Adachi O
  Title
Intramolecular electron transport in quinoprotein alcohol dehydrogenase of Acetobacter methanolicus: a redox-titration study
  Journal
Biochim Biophys Acta 1363:24-34 (1998)
DOI:10.1016/S0005-2728(97)00090-X
Reference
5  [PMID:18838797]
  Authors
Matsushita K, Kobayashi Y, Mizuguchi M, Toyama H, Adachi O, Sakamoto K, Miyoshi H
  Title
A tightly bound quinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase of an acetic acid bacterium, Gluconobacter suboxydans.
  Journal
Biosci Biotechnol Biochem 72:2723-31 (2008)
DOI:10.1271/bbb.80363
Reference
6  [PMID:8617755]
  Authors
Matsushita K, Yakushi T, Toyama H, Shinagawa E, Adachi O
  Title
Function of multiple heme c moieties in intramolecular electron transport and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase-cytochrome c complex of Gluconobacter suboxydans.
  Journal
J Biol Chem 271:4850-7 (1996)
DOI:10.1074/jbc.271.9.4850
Reference
7
  Authors
Matsushita, K., Takaki, Y., Shinagawa, E., Ameyama, M. and Adachi, O.
  Title
Ethanol oxidase respiratory chain of acetic acid bacteria. Reactivity with ubiquinone of pyrroloquinolinequinone-dependent alcohol dehydrogenases purified from Acetobacter aceti and Gluconobacter suboxydans.
  Journal
Biosci Biotechnol Biochem 56:304-310 (1992)
Reference
8  [PMID:7942316]
  Authors
Matsushita K, Toyama H, Adachi O
  Title
Respiratory chains and bioenergetics of acetic acid bacteria.
  Journal
Adv Microb Physiol 36:247-301 (1994)
DOI:10.1016/s0065-2911(08)60181-2
Reference
9  [PMID:7772016]
  Authors
Cozier GE, Giles IG, Anthony C
  Title
The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens.
  Journal
Biochem J 308 ( Pt 2):375-9 (1995)
DOI:10.1042/bj3080375
Other DBs
ExplorEnz - The Enzyme Database: 1.1.5.5
IUBMB Enzyme Nomenclature: 1.1.5.5
ExPASy - ENZYME nomenclature database: 1.1.5.5
BRENDA, the Enzyme Database: 1.1.5.5
LinkDB

DBGET integrated database retrieval system