Entry
Name
(R)-2-hydroxyacyl-CoA dehydratase activating ATPase;
archerase;
(R)-2-hydroxyacyl-CoA dehydratase activator;
(R)-2-hydroxyacyl-CoA dehydratase activase;
fldI (gene name);
hgdC (gene name);
hadI (gene name);
lcdC (gene name)
Class
Isomerases;
Isomerases altering macromolecular conformation;
Enzymes altering polypeptide conformation or assembly
BRITE hierarchy
Sysname
reduced flavodoxin:(R)-2-hydroxyacyl-CoA dehydratase electron transferase (ATP-hydrolyzing)
Reaction(IUBMB)
2 ATP + a reduced flavodoxin + an inactive (R)-2-hydroxyacyl-CoA dehydratase + 2 H2O = 2 ADP + 2 phosphate + a flavodoxin semiquinone + an active (R)-2-hydroxyacyl-CoA dehydratase
Substrate
ATP [CPD:
C00002 ];
reduced flavodoxin [CPD:
C02745 ];
inactive (R)-2-hydroxyacyl-CoA dehydratase;
H2O [CPD:
C00001 ]
Product
ADP [CPD:
C00008 ];
phosphate [CPD:
C00009 ];
flavodoxin semiquinone [CPD:
C05199 ];
active (R)-2-hydroxyacyl-CoA dehydratase
Comment
Members of the (R)-2-hydroxyacyl-CoA dehydratase family (including EC
4.2.1.54 , lactoyl-CoA dehydratase, EC
4.2.1.157 , (R)-2-hydroxyisocaproyl-CoA dehydratase, EC
4.2.1.167 , (R)-2-hydroxyglutaryl-CoA dehydratase and EC
4.2.1.175 , (R)-3-(aryl)lactoyl-CoA dehydratase) are two-component systems composed of an activator component and a dehydratase component. The activator is an extremely oxygen-sensitive homodimer with one [4Fe-4S] cluster bound at the dimer interface. Before it can catalyse the dehydration reaction, the dehydratase requires one high-energy electron that is used to transiently reduce the electrophilic thiol ester carbonyl to a nucleophilic ketyl radical anion, facilitating the elimination of the hydroxyl group. The activator, which has been named archerase because its open position resembles an archer shooting arrows, binds two ADP molecules. Upon the reduction of its [4Fe-4S] cluster by a single electron, delivered by a dedicated flavodoxin or a clostridial ferredoxin, the two ADP molecules exchange for two ATP molecules, resulting in a large conformational change. The change allows the activator to bind to the dehydratase component and transfer the electron to it, activating it. During this event the two ATP molecules are hydrolysed and the activator returns to its resting state. Since the electron is regenerated at the end of each reaction cycle of the dehydratase, the activation is required only once, before the first reaction takes place.
History
EC 5.6.1.9 created 2019
Orthology
K23876 (R)-2-hydroxyacyl-CoA dehydratese activating ATPase
Genes
THIC : TspCOW1_00970(hadI)
AZI : AzCIB_4490 AzCIB_4491
AZD : CDA09_21810 CDA09_21815
DDZ : DSYM_18990 DSYM_19000
MAGX : XM1_2275(hgdC) XM1_2276
SULC : CVO_01310 CVO_01645
SMAB : LN246_02385 LN246_15025
GSU : GSU2520(yjiL) GSU2926 GSU2945
GSK : KN400_2465(yjiL) KN400_2869 KN400_2889
GAO : A2G06_05010 A2G06_13800
GBZ : JZM60_08345 JZM60_11070
GLO : Glov_0090 Glov_2398 Glov_2399
GBM : Gbem_0392 Gbem_1412 Gbem_2039(yjiL)
GBN : GEOBRER4_03830 GEOBRER4_18640(yjiL)
GER : KP004_01100 KP004_09200 KP004_19480
GSUB : KP001_05975 KP001_14360 KP001_16830
GNT : KP003_00800 KP003_08610 KP003_19480
GPL : M1B72_00275 M1B72_19790
PACE : A6070_09580 A6070_13405 A6070_14235
DHY : DESAM_20189 DESAM_23254
DAT : HRM2_43020(hgdC1) HRM2_43460(hgdC2)
DTO : TOL2_C39520(hgdC) TOL2_C39530(hgdC2)
DOV : DSCO28_17060 DSCO28_25240(fldI_1) DSCO28_26150 DSCO28_26160 DSCO28_29450 DSCO28_30030(hadI) DSCO28_31330(fldI_2) DSCO28_47730
DWD : DSCW_14430 DSCW_27270 DSCW_40270
DALK : DSCA_13470 DSCA_25480 DSCA_45710
DVR : Dvar_16090 Dvar_16700 Dvar_74990 Dvar_83490 Dvar_83720
DML : Dmul_15150(hgdC) Dmul_24860
DMM : dnm_010930 dnm_025900 dnm_068880
DEK : DSLASN_23170(hadI) DSLASN_25880
DTI : Desti_1563 Desti_3028
SHYR : LA303_09480 LA303_10130
CNO : NT01CX_2370(hgdC) NT01CX_2383
CBO : CBO1553 CBO2192(hadI) CBO3242 CBO3291(fldI)
CBA : CLB_1574(hgdC-1) CLB_2130(hgdC-2) CLB_3279(hgdC) CLB_3347(fldI)
CBH : CLC_1585(hgdC-1) CLC_2135(hgdC-2) CLC_3153(hgdC) CLC_3233(fldI)
CBY : CLM_1794(hgdC) CLM_2393(hgdC_1) CLM_3655(hgdC_2) CLM_3724(fldI)
CBL : CLK_1032 CLK_1630 CLK_2640(hgdC) CLK_2707(fldI)
CBB : CLD_1232(fldI) CLD_1289(hgdC) CLD_2388 CLD_2999
CBI : CLJ_B1663 CLJ_B2400 CLJ_B3516(hgdC) CLJ_B3571(fldI)
CBN : CbC4_0486(hgdC) CbC4_1684
CBF : CLI_1635(hgdC-1) CLI_2235(hgdC-2) CLI_3381 CLI_3461(fldI)
CBM : CBF_2220 CBF_3374 CBF_3443(fldI)
CBJ : H04402_01620 H04402_02201 H04402_03330 H04402_03376
CPAE : CPAST_c16330(fldI1)
CLD : CLSPO_c15960(fldI2) CLSPO_c22240(lcdC) CLSPO_c33450 CLSPO_c34110(fldI1)
CACE : CACET_c07720(hgdC3) CACET_c29250(hgdC4)
CCK : Ccar_00145 Ccar_18320
CFM : BJL90_00170 BJL90_20700
CARG : RSJ17_01745 RSJ17_16375
CFER : D4Z93_03850 D4Z93_06610
CCAA : KQH81_01445 KQH81_14405
CRW : CROST_000360(fldI_1)
CAUN : CLAUR_029590(fldI_2)
CTAG : LL095_04825 LL095_05885 LL095_07990
HHW : NCTC503_00354(hgdC_2)
CRS : FQB35_02240 FQB35_14945
CPRF : K7H06_05580 K7H06_13625 K7H06_15135 K7H06_19885
OCW : OW730_19750 OW730_26540
CLO : HMPREF0868_0585(hgdC)
OVA : OBV_10870(hgdC) OBV_24200
CAPR : EQM14_01975 EQM14_09400 EQM14_12240
CFEM : HCR03_03850 HCR03_16265 HCR03_18560
SWO : Swol_0411 Swol_0428 Swol_0452
SALQ : SYNTR_0051 SYNTR_0280
DSY : DSY2314 DSY2745 DSY3231
DHD : Dhaf_3452 Dhaf_3911 Dhaf_4398
DDH : Desde_2888 Desde_3353 Desde_3777
DDL : Desdi_3109 Desdi_3306
DOR : Desor_1725 Desor_2862 Desor_3091 Desor_4352 Desor_4925 Desor_5273
DAI : Desaci_0243 Desaci_2301 Desaci_4371
DMI : Desmer_1676 Desmer_1799 Desmer_3945 Desmer_4257
DCA : Desca_0606 Desca_0788
DRU : Desru_0929 Desru_2799
DFG : B0537_06110 B0537_13805
DAE : Dtox_0118 Dtox_1468 Dtox_3624
DKU : Desku_0369 Desku_2120
FWA : DCMF_12855 DCMF_24445
AACX : DEACI_0126 DEACI_1857 DEACI_2684
TJR : TherJR_0858 TherJR_2569
HMO : HM1_0162(hgdC) HM1_0462(hgdC)
HCV : FTV88_0886 FTV88_3306
IBU : IB211_02384c IB211_02574
PROM : QO263_14210 QO263_17870
CSCI : HDCHBGLK_01326(hgdC)
CSH : Closa_0478 Closa_3012
LGG : QJR73_04940 QJR73_06895
MDV : C5Q96_01390 C5Q96_07280
MNL : QU661_02655 QU661_08055
ETM : CE91St48_25630(hadI)
GFE : Gferi_06495 Gferi_18145
CSPO : QNI18_03105 QNI18_07880
PBIF : KXZ80_01465 KXZ80_06090
PSOR : RSJ16_06935 RSJ16_16050
CDF : CD630_03960(hadI) CD630_17500
PDC : CDIF630_00524(hadI) CDIF630_01944(yjiL)
CDC : CD196_0381(hadI) CD196_1669(hgdC)
CDL : CDR20291_0367(hadI) CDR20291_1644(hgdC)
PDF : CD630DERM_03960(hadI) CD630DERM_17500
PHX : KGNDJEFE_01110(hadI_1)
TEB : T8CH_0921(yjiL) T8CH_2922
THYR : P4S50_02440 P4S50_12490 P4S50_17120
PEB : O0R46_02450 O0R46_05215
EAC : EAL2_c06780(hgdC1) EAL2_c15350(yjiL)
FAA : HMPREF0389_01472(hgdC)
CHY : CHY_0311 CHY_0488 CHY_0848(hgdC)
MTHO : MOTHE_c09620(fldI1) MOTHE_c14070(fldI4)
MTHZ : MOTHA_c10510(fldI1) MOTHA_c14930(fldI4)
DBC : MFMK1_001009 MFMK1_002227
NTH : Nther_0829 Nther_1773
AAR : Acear_1412 Acear_2284 Acear_2297
PHAR : NCTC13077_00177(hgdC_1)
PIV : NCTC13079_00075(hgdC_1) NCTC13079_01305(hgdC_3)
MHAP : JFY71_01805 JFY71_11620
CAD : Curi_c04300 Curi_c26040(hgdC2)
CAZO : G3A45_00415 G3A45_12855
MANA : MAMMFC1_00643(hgdC_2) MAMMFC1_02512(fldI_6) MAMMFC1_02612(fldI_7)
STED : SPTER_06770(hadI_1) SPTER_10580(hadI_2)
SSPH : SPSPH_006920(fldI) SPSPH_031830(hadI)
SOVA : SOV_11520(fldI_1) SOV_25330(fldI_2) SOV_47110(hgdC_4)
SSID : SPSIL_012380(hadI_1) SPSIL_016440(fldI)
SACV : SPACI_012170(hadI_1) SPACI_016980(hadI_3) SPACI_022540(hgdC)
EYY : EGYY_02510 EGYY_07660
PPIO : CE91St28_00780 CE91St28_02610(hgdC)
PYY : RAH42_00955 RAH42_03390
FNF : BSQ88_06940 BSQ88_08510
FPOL : ERS445057_00634(hgdC_1)
MFS : MFS40622_0127 MFS40622_0205
LOKI : Lokiarch_29240(hgdC_2)
» show all
Taxonomy
Reference
Authors
Bendrat K, Muller U, Klees AG, Buckel W
Title
Identification of the gene encoding the activator of (R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans by gene expression in Escherichia coli.
Journal
Sequence
Reference
Authors
Muller U, Buckel W
Title
Activation of (R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans.
Journal
Sequence
Reference
Authors
Locher KP, Hans M, Yeh AP, Schmid B, Buckel W, Rees DC
Title
Crystal structure of the Acidaminococcus fermentans 2-hydroxyglutaryl-CoA dehydratase component A.
Journal
Sequence
Reference
Authors
Dickert S, Pierik AJ, Buckel W
Title
Molecular characterization of phenyllactate dehydratase and its initiator from Clostridium sporogenes.
Journal
Sequence
Reference
Authors
Thamer W, Cirpus I, Hans M, Pierik AJ, Selmer T, Bill E, Linder D, Buckel W
Title
A two [4Fe-4S]-cluster-containing ferredoxin as an alternative electron donor for 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans.
Journal
Reference
Authors
Kim J, Hetzel M, Boiangiu CD, Buckel W
Title
Dehydration of (R)-2-hydroxyacyl-CoA to enoyl-CoA in the fermentation of alpha-amino acids by anaerobic bacteria.
Journal
Reference
Authors
Kim J, Darley D, Buckel W
Title
2-Hydroxyisocaproyl-CoA dehydratase and its activator from Clostridium difficile.
Journal
Sequence
Reference
Authors
Kim J, Darley DJ, Buckel W, Pierik AJ
Title
An allylic ketyl radical intermediate in clostridial amino-acid fermentation.
Journal
Reference
Authors
Knauer SH, Buckel W, Dobbek H
Title
On the ATP-dependent activation of the radical enzyme (R)-2-hydroxyisocaproyl-CoA dehydratase.
Journal
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 5.6.1.9
ExPASy - ENZYME nomenclature database: 5.6.1.9
BRENDA, the Enzyme Database: 5.6.1.9