Entry
Name
alcohol dehydrogenase (azurin);
type II quinoprotein alcohol dehydrogenase;
quinohaemoprotein ethanol dehydrogenase;
QHEDH;
ADHIIB
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With a copper protein as acceptor
BRITE hierarchy
Sysname
alcohol:azurin oxidoreductase
Reaction(IUBMB)
a primary alcohol + azurin = an aldehyde + reduced azurin [RN:
R09480 ]
Reaction(KEGG)
Substrate
primary alcohol [CPD:
C00226 ];
azurin
Product
Comment
A soluble, periplasmic PQQ-containing quinohemoprotein. Also contains a single heme c. Occurs in Comamonas and Pseudomonas. Does not require an amine activator. Oxidizes a wide range of primary and secondary alcohols, and also aldehydes and large substrates such as sterols; methanol is not a substrate. Usually assayed with phenazine methosulfate or ferricyanide. 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 disulfide ring structure in close proximity to the PQQ.
History
EC 1.1.9.1 created 2010 as EC 1.1.98.1; transferred 2011 to EC 1.1.9.1
Orthology
K17760 quinohemoprotein ethanol dehydrogenase
Genes
PCQ : PcP3B5_33080(qgdA_1)
PQI : KH389_15205 KH389_15915 KH389_17020
PTAE : NCTC10697_01924(qheDH)
PPHN : HU825_14525 HU825_15730
PCAS : LOY40_16600 LOY40_17405 LOY40_17685
PSED : DM292_04320 DM292_07550
PCHL : LLJ08_06255 LLJ08_09455
SDEG : GOM96_01520 GOM96_02720
PSPI : PS2015_1348 PS2015_2383
SNAN : I6N98_04765 I6N98_07195 I6N98_13860
ZAL : AZF00_00410 AZF00_02915 AZF00_06825
OSG : BST96_06520 BST96_11945 BST96_14245 BST96_17020
KIM : G3T16_00650 G3T16_16955
AFUS : EYZ66_01320 EYZ66_01385 EYZ66_03410 EYZ66_03590 EYZ66_06330
ALCA : ASALC70_00253(qgdA) ASALC70_03961(qheDH)
SOK : D0B54_04380 D0B54_04385
FCE : JN531_004925 JN531_005045
REH : H16_A1884(h16_A1884)
CNC : CNE_1c18660(qheDH) CNE_BB1p04310(adh)
REU : Reut_A1461 Reut_B4160
CCUP : BKK81_18975 BKK81_27650
CUP : BKK80_22965 BKK80_28675
CUU : BKK79_28240 BKK79_34625
CNAN : A2G96_11225 A2G96_12165
DLA : I6G47_06900 I6G47_09325
CTT : CtCNB1_0197 CtCNB1_1388
METP : C1M51_13570 C1M51_13725
ATER : MW290_13615 MW290_24600
DOE : DENOEST_0490(qbdA) DENOEST_2039(qbdA) DENOEST_3548(qbdA) DENOEST_3675(qbdA)
AZR : CJ010_18755 CJ010_22255
RBS : RHODOSMS8_03066(qbdA)
VGO : GJW-30_1_04338(qheDH)
CAUL : KCG34_00855 KCG34_05195
TSV : DSM104635_00613(qgdA)
NPP : PP1Y_AT11408 PP1Y_AT11547 PP1Y_Mpl5286
NRE : BES08_11360 BES08_19965 BES08_22630 BES08_27330
NOV : TQ38_020540 TQ38_024820
NOT : C7W88_07620 C7W88_07660
NOR : FA702_09260 FA702_10240 FA702_20765
NDR : HT578_07545 HT578_07615 HT578_09220 HT578_14485
SMAG : AN936_03210 AN936_16350
SMAZ : LH19_18005 LH19_18030 LH19_18835
SINA : KNJ79_14270 KNJ79_15265
SWI : Swit_0721 Swit_1001 Swit_2227 Swit_5136
SPHD : HY78_14390 HY78_21510 HY78_23090
RDI : CMV14_16905 CMV14_19410
SBIN : SBA_ch2_6170 SBA_ch2_6490
SNAP : PQ455_02615 PQ455_04140
SJP : SJA_C1-02010 SJA_C1-02070 SJA_C2-04000
SINB : SIDU_17200 SIDU_17230
SCH : Sphch_0592 Sphch_0603 Sphch_2127
SSY : SLG_05620 SLG_07280 SLG_12260 SLG_12290 SLG_18610 SLG_20920
SYB : TZ53_16615 TZ53_17030 TZ53_17090
SPHB : EP837_00323 EP837_00335(exaA) EP837_03710
SPHR : BSY17_3920(qbdA) BSY17_934(qbdA)
SPHT : K426_12160 K426_12220
SHYD : CJD35_16290 CJD35_16630 CJD35_20620
SYA : A6768_05740 A6768_05805 A6768_20115
SCLO : SCLO_1006180 SCLO_1006300
SPYG : YGS_C2P0050 YGS_C2P0418
SUFL : FIL70_03770 FIL70_05365 FIL70_05425
SBAR : H5V43_00800 H5V43_04645 H5V43_05050 H5V43_05110
SAMI : SAMIE_1016260 SAMIE_1019310
SPPH : KFK14_04690 KFK14_08020 KFK14_10340 KFK14_13445 KFK14_17040
SPHG : AZE99_03780 AZE99_04575 AZE99_04655
SFLA : SPHFLASMR4Y_01514(qbdA)
SLAA : EUU25_00640 EUU25_15690
BLAS : BSY18_3165(adhA) BSY18_3429(qgdA)
BFW : B5J99_06725 B5J99_07940
SPHJ : BSL82_14255 BSL82_14300
ACOB : P0Y56_05660 P0Y56_09930 P0Y56_12020 P0Y56_13035 P0Y56_15910 P0Y56_16520 P0Y56_16555
SMIC : SmB9_16520 SmB9_26030(exaA) SmB9_32770
ALB : AEB_P1071 AEB_P2933 AEB_P2938
ALH : G6N82_06175 G6N82_10280
AAY : WYH_01144(qbdA_1) WYH_01921(qbdA_3) WYH_02888(qbdA_4) WYH_03122(qgdA) WYH_03187(qbdA_5)
ERF : FIU90_00555(qbdA1) FIU90_08125(qbdA2)
NTD : EGO55_06120 EGO55_07055
ECOG : FIV45_03450 FIV45_11680
ABAC : LuPra_01740(qgdA_1) LuPra_02092(qbdA_3)
LUB : TBR22_A09890 TBR22_A16680(exaA_1)
» show all
Taxonomy
Reference
Authors
Groen BW, van Kleef MA, Duine JA
Title
Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni.
Journal
Reference
Authors
de Jong GA, Caldeira J, Sun J, Jongejan JA, de Vries S, Loehr TM, Moura I, Moura JJ, Duine JA
Title
Characterization of the interaction between PQQ and heme c in the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni.
Journal
Reference
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
Reference
Authors
Matsushita K, Yamashita T, Aoki N, Toyama H, Adachi O
Title
Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory chain of Pseudomonas putida HK5.
Journal
Reference
Authors
Chen ZW, Matsushita K, Yamashita T, Fujii TA, Toyama H, Adachi O, Bellamy HD, Mathews FS
Title
Structure at 1.9 A resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5.
Journal
Sequence
Reference
Authors
Oubrie A, Rozeboom HJ, Kalk KH, Huizinga EG, Dijkstra BW
Title
Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer.
Journal
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.1.9.1
ExPASy - ENZYME nomenclature database: 1.1.9.1
BRENDA, the Enzyme Database: 1.1.9.1