KEGG   ENZYME: 1.1.2.8Help
Entry
EC 1.1.2.8                  Enzyme                                 
Name
alcohol dehydrogenase (cytochrome c);
type I quinoprotein alcohol dehydrogenase;
quinoprotein ethanol dehydrogenase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With a cytochrome as acceptor
BRITE hierarchy
Sysname
alcohol:cytochrome c oxidoreductase
Reaction(IUBMB)
a primary alcohol + 2 ferricytochrome c = an aldehyde + 2 ferrocytochrome c + 2 H+
Reaction(KEGG)
Substrate
primary alcohol [CPD:C00226];
ferricytochrome c [CPD:C00125]
Product
aldehyde [CPD:C00071];
ferrocytochrome c [CPD:C00126];
H+ [CPD:C00080]
Comment
A periplasmic PQQ-containing quinoprotein. Occurs in Pseudomonas and Rhodopseudomonas. The enzyme from Pseudomonas aeruginosa uses a specific inducible cytochrome c550 as electron acceptor. Acts on a wide range of primary and secondary alcohols, but not methanol. It has a homodimeric structure [contrasting with the heterotetrameric structure of EC 1.1.2.7, methanol dehydrogenase (cytochrome c)]. It is routinely assayed with phenazine methosulphate as electron acceptor. Activity is stimulated by ammonia or amines. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulphide ring structure in close proximity to the PQQ.
Pathway
Glycolysis / Gluconeogenesis
Chloroalkane and chloroalkene degradation
Propanoate metabolism
Metabolic pathways
Biosynthesis of secondary metabolites
Microbial metabolism in diverse environments
Orthology
K00114  
alcohol dehydrogenase (cytochrome c)
Genes
FAU: 
PAE: 
PA1982(exaA)
PAU: 
PAP: 
PAG: 
PAF: 
PNC: 
PDK: 
PSG: 
PPU: 
PPF: 
Pput_3084 Pput_3089
PPG: 
PputGB1_3124 PputGB1_3129
PPW: 
PputW619_2696
PPT: 
PPS_2221 PPS_2226
PPB: 
PPUBIRD1_2997 PPUBIRD1_3002(qedH)
PPI: 
YSA_09633 YSA_09642
PPX: 
T1E_2678(exaA) T1E_2683
PPUH: 
B479_11520 B479_11545
PPUU: 
PputUW4_02943
PFL: 
PFL_2216(pedE) PFL_2221(pedH)
PFE: 
PSF113_2976 PSF113_2981
PMY: 
Pmen_1957 Pmen_1963
PMK: 
MDS_2680 MDS_2937 MDS_2944
PSA: 
PST_2265 PST_2270
PSZ: 
PSTAB_2150 PSTAB_2156 PSTAB_2905
PSR: 
PSTAA_2293 PSTAA_2299 PSTAA_3020
PSC: 
A458_09430 A458_09460
PSJ: 
PSJM300_09490
PSH: 
Psest_1423 Psest_2054 Psest_2060
PBA: 
PSEBR_a2660 PSEBR_a2665
SWD: 
Swoo_2255
CPS: 
CPS_1887(exaA)
PAT: 
Patl_1855
MHC: 
MARHY3265(exaA) MARHY3268(exaA)
MAD: 
HP15_3160 HP15_3164
MBS: 
MRBBS_1203(exaA)
AMAC: 
MASE_05380 MASE_15465
AMB: 
AMBAS45_05580 AMBAS45_15905
AMG: 
AMEC673_05455 AMEC673_15760
AMK: 
AMBLS11_15210
AMAA: 
amad1_16415
ALT: 
ambt_01200
GAG: 
Glaag_1842
GPS: 
C427_3776
CYQ: 
Q91_2236(exaA)
NHL: 
Nhal_3866
AEH: 
Mlg_2729
ADI: 
B5T_01640 B5T_04379(exaA1)
PSE: 
NH8B_3445
RPI: 
Rpic_2494
RPF: 
Rpic12D_2100
REU: 
Reut_A1784 Reut_B4160
REH: 
H16_A1884(h16_A1884) H16_B1047(quiA)
CTI: 
RALTA_A1577(exaA1) RALTA_B0666(exaA2)
CNC: 
CNE_1c18660(qheDH) CNE_2c10080(quiA) CNE_BB1p04310(adh)
BVI: 
Bcep1808_6562
BCN: 
Bcen_3242
BCH: 
Bcen2424_5126
BCM: 
Bcenmc03_5155
BCJ: 
BCAM2368
BAM: 
Bamb_6162
BAC: 
BamMC406_5895
BMU: 
Bmul_5972
BMJ: 
BMULJ_05554
BXE: 
Bxe_B0306
BPH: 
Bphy_7192
BUG: 
BC1001_4980
BGE: 
BC1002_1266
BGF: 
BC1003_4493
BYI: 
BYI23_D007680
BUK: 
MYA_5958
BPX: 
BUPH_01542
POL: 
Bpro_5302
PNA: 
Pnap_0726
VEI: 
Veis_0427
DAC: 
Daci_3352
DEL: 
DelCs14_3417
VAP: 
Vapar_5018 Vapar_6242
VPE: 
Varpa_5729
CTT: 
CtCNB1_0197 CtCNB1_1388
MPT: 
Mpe_A0473 Mpe_A0476 Mpe_A0877 Mpe_A0905
LCH: 
Lcho_1811
THI: 
THI_0488
AZO: 
azo2844(exaA1) azo2972(exaA2) azo2975(exaA3) azo3022(exaA4)
AZA: 
AZKH_1557 AZKH_p0287
DAR: 
Daro_1023
TMZ: 
Tmz1t_2817
SULR: 
B649_05170
ANT: 
Arnit_2785
PLA: 
Plav_1306
SMD: 
Smed_6351
RHI: 
NGR_b03250
SFH: 
SFHH103_06439(exaA)
SFD: 
USDA257_c26010(exaA)
BJA: 
blr6207(exaA)
BJU: 
BJ6T_34810 BJ6T_34960 BJ6T_73570
BRA: 
BRADO5480
BBT: 
BBta_5502 BBta_5964
BRS: 
S23_20730 S23_20880(exaA)
RPA: 
RPA3188
RPB: 
RPB_2355
RPD: 
RPD_3110
RPE: 
RPE_3525
RPT: 
Rpal_3601
RPX: 
Rpdx1_2242
AOL: 
S58_22280 S58_31370
XAU: 
Xaut_1781
MEX: 
Mext_1339
MEA: 
Mex_1p1139(exa)
MDI: 
METDI1985(exa)
MCH: 
Mchl_1540
MRD: 
Mrad2831_2409
MET: 
M446_3624
MPO: 
Mpop_4873
BID: 
Bind_3639
MSL: 
Msil_3387
HDN: 
Hden_0340
HDT: 
HYPDE_34983
HMC: 
HYPMC_3613 HYPMC_4861(adh)
RVA: 
Rvan_1822
PHL: 
KKY_1072 KKY_1190 KKY_201 KKY_351
PZU: 
PHZ_c3112
SIL: 
SPO1508
RCP: 
RCAP_rcc01396(exaA1) RCAP_rcc01657(exaA2)
DSH: 
Dshi_2673(exaA)
KVL: 
KVU_0632 KVU_PA0245
HNE: 
HNE_0129(adhA)
NAR: 
Saro_2870
NPP: 
PP1Y_AT11547 PP1Y_AT5722 PP1Y_Mpl5286
SAL: 
Sala_0379
SWI: 
Swit_0693 Swit_0721 Swit_5136
SJP: 
SJA_C1-02010 SJA_C1-02070 SJA_C2-04000 SJA_C2-05730
SCH: 
Sphch_0603 Sphch_2127
SSY: 
SLG_05620 SLG_12260 SLG_20920
ELI: 
ELI_14570
GOX: 
GOX1068
GOH: 
B932_1062
GBE: 
GbCGDNIH1_1922
ACR: 
Acry_1741
AMV: 
ACMV_17860
GDI: 
GDI_2040(adhA)
GDJ: 
Gdia_0262
GXY: 
GLX_26610
APT: 
APA01_00870 APA01_22100
APW: 
APA42C_00870 APA42C_22100
APF: 
APA03_00870 APA03_22100
APU: 
APA07_00870 APA07_22100
APG: 
APA12_00870 APA12_22100
APQ: 
APA22_00870 APA22_22100
APX: 
APA26_00870 APA26_22100
APZ: 
APA32_00870 APA32_22100
AZL: 
AZL_a05260 AZL_b04560
ALI: 
AZOLI_p20241 AZOLI_p20409(exaA)
ABS: 
AZOBR_180211(exaA) AZOBR_p330074
MSM: 
MSMEG_3726
MSG: 
MSMEI_3638
SHY: 
SHJG_2432
SHO: 
SHJGH_2197
GOB: 
Gobs_2451
SEN: 
SACE_4449(exaA)
PDX: 
Psed_0735
TSA: 
AciPR4_0226 AciPR4_0416 AciPR4_2733
TRS: 
Terro_0082 Terro_2792 Terro_4026
SUS: 
Acid_6912
HTH: 
HTH_0392
HTE: 
Hydth_0390
NPE: 
Natpe_2907
NOU: 
Natoc_1762
 » show all
Taxonomy
Reference
1  [PMID:3144289]
  Authors
Rupp M, Gorisch H
  Title
Purification, crystallisation and characterization of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa.
  Journal
Biol. Chem. Hoppe. Seyler. 369 (1988) 431-9.
Reference
2  [PMID:7730276]
  Authors
Toyama H, Fujii A, Matsushita K, Shinagawa E, Ameyama M, Adachi O
  Title
Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols.
  Journal
J. Bacteriol. 177 (1995) 2442-50.
Reference
3  [PMID:10075429]
  Authors
Schobert M, Gorisch H
  Title
Cytochrome c550 is an essential component of the quinoprotein ethanol oxidation system in Pseudomonas aeruginosa: cloning and sequencing of the genes encoding cytochrome c550 and an adjacent acetaldehyde dehydrogenase.
  Journal
Microbiology. 145 ( Pt 2) (1999) 471-81.
Reference
4  [PMID:10736230]
  Authors
Keitel T, Diehl A, Knaute T, Stezowski JJ, Hohne W, Gorisch H
  Title
X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity.
  Journal
J. Mol. Biol. 297 (2000) 961-74.
Reference
5  [PMID:15094044]
  Authors
Kay CW, Mennenga B, Gorisch H, Bittl R
  Title
Characterisation of the PQQ cofactor radical in quinoprotein ethanol dehydrogenase of Pseudomonas aeruginosa by electron paramagnetic resonance spectroscopy.
  Journal
FEBS. Lett. 564 (2004) 69-72.
Reference
6  [PMID:19224199]
  Authors
Mennenga B, Kay CW, Gorisch H
  Title
Quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: the unusual disulfide ring formed by adjacent cysteine residues is essential for efficient electron transfer to cytochrome c550.
  Journal
Arch. Microbiol. 191 (2009) 361-7.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
DBGET integrated database retrieval system