KEGG   ENZYME: 5.6.1.9
Entry
EC 5.6.1.9                  Enzyme                                 

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
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
EAL: EAKF1_ch2939
PMIB: BB2000_2636
PVL: AOB99_14465
PVG: CRN77_06460
PHAU: PH4a_04705
PROT: BTA34_14445
PCOL: F1325_16660
PCIB: F9282_17005
HAV: AT03_18345
OPO: DSM2777_07055
AEH: Mlg_0786
AHA: AHA_3542
GCA: Galf_2621
SLAC: SKTS_00550(hadI)
ABRE: pbN1_02460(hgdC)
APET: ToN1_03310
WSU: WS0738
CGRA: CGRAC_1814(hgdC)
AMYT: AMYT_1140
AMAR: AMRN_1038
ACAA: ACAN_1087
AMOL: AMOL_1014
HEBR: AEBR_1326
SDL: Sdel_2023
SMUL: SMUL_2812
SHAL: SHALO_2587
SULJ: SJPD1_2494
GME: Gmet_0544
GEB: GM18_0484
PCA: Pcar_2727
PPD: Ppro_1277
DVL: Dvul_0705
DVM: DvMF_0987
DDE: Dde_0089
DDS: Ddes_0546
DMA: DMR_06590(hgdC)
DGG: DGI_1311
DFL: DFE_2246
DAS: Daes_1017
DPI: BN4_10682
PPRF: DPRO_3457(fldI)
DBA: Dbac_1928
DPS: DP2514
DAT: HRM2_43020(hgdC1) HRM2_43460(hgdC2)
DTO: TOL2_C39520(hgdC) TOL2_C39530(hgdC2)
DLI: dnl_46440
SAT: SYN_00371
SFU: Sfum_3160
DBR: Deba_0558
RPC: RPC_2057
RVA: Rvan_3618
SMAZ: LH19_27075
MAGX: XM1_2275(hgdC) XM1_2276
PSAB: PSAB_11715
CAE: SMB_G3664(hgdC)
CAY: CEA_G3630
CBO: CBO2192(hadI) 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 CLC_3233(fldI)
CBY: CLM_1794(hgdC) CLM_2393(hgdC_1) CLM_3655(hgdC_2) CLM_3724(fldI)
CBK: CLL_A0649(hgdC)
CBN: CbC4_0486(hgdC) CbC4_1684
CBT: CLH_0609(hgdC)
CBF: CLI_1635(hgdC-1) CLI_2235(hgdC-2) CLI_3381 CLI_3461(fldI)
CKL: CKL_0423
CKR: CKR_0368
CPAS: Clopa_3176
CPAT: CLPA_c16330(fldI1)
CPAE: CPAST_c16330(fldI1)
CLT: CM240_3180(fldI2)
CSQ: CSCA_4630
CACE: CACET_c07720(hgdC3) CACET_c29250(hgdC4)
CTYK: CTK_C06850(fldI)
AMT: Amet_3210
AOE: Clos_2148
HHW: NCTC503_00354(hgdC_2)
CLO: HMPREF0868_0585(hgdC)
CTH: Cthe_3104
HSC: HVS_12040(fldI1)
OVA: OBV_10870(hgdC) OBV_24200
BPB: bpr_I1766(hgdC)
BFI: CIY_10650
BPRO: PMF13cell1_04708(hadI_2)
CSCI: HDCHBGLK_01326(hgdC)
CSO: CLS_16280
CPRO: CPRO_08370(fldI)
EHL: EHLA_2907
RTO: RTO_22540
CDF: CD630_03960(hadI)
PDC: CDIF630_00524(hadI)
CDC: CD196_0381(hadI)
CDL: CDR20291_0367(hadI)
PDF: CD630DERM_03960(hadI)
EAC: EAL2_c06780(hgdC1)
FAA: HMPREF0389_01472(hgdC)
PTH: PTH_0568
DAU: Daud_0885
SGY: Sgly_1017
HMO: HM1_0162(hgdC) HM1_0462(hgdC)
AWO: Awo_c08280(hgdC)
BPRS: CK3_23960
MTHO: MOTHE_c09620(fldI1) MOTHE_c14070(fldI4)
MTHZ: MOTHA_c10510(fldI1) MOTHA_c14930(fldI4)
ADG: Adeg_1706
TPZ: Tph_c09670(hgdC1)
TACI: TDSAC_1539
FMA: FMG_1201
PMIC: NW74_06355
PED: ING2D1G_1421(hgdC)
PHAR: NCTC13077_00177(hgdC_1)
PIV: NCTC13079_00075(hgdC_1) NCTC13079_01305(hgdC_3)
CAD: Curi_c26040(hgdC2)
MED: MELS_0744
PFT: JBW_01502
MANA: MAMMFC1_00154(fldI_2) MAMMFC1_00643(hgdC_2) MAMMFC1_00664(fldI_4) MAMMFC1_02512(fldI_6) MAMMFC1_02612(fldI_7)
STED: SPTER_05630(hgdC) SPTER_06770(hadI_1) SPTER_10580(hadI_2)
AIN: Acin_0319
GOM: D7316_03197(hadI_1) D7316_03205(hadI_2)
GPA: GPA_28540
CBAC: JI75_01415
ALUS: STSP2_01368(hgdC)
TPED: TPE_0433(hgdC)
BRM: Bmur_0619
BPW: WESB_2052
FNU: FN0206
TAI: Taci_0253
SBR: SY1_11830
MBAS: ALGA_3946
CACI: CLOAM0918(hgdC)
TTK: TST_0185(hgdC)
DTU: Dtur_1745
MMD: GYY_01790
MMAK: MMKA1_03590(hadI)
MMAO: MMOS7_03830(hadI)
MMAD: MMJJ_07070(fldI_2)
MAE: Maeo_1347
MVO: Mvol_1674
MKA: MK0260
FPL: Ferp_1041
GAC: GACE_0788
MBAK: MSBR3_2406
MTHR: MSTHT_0968
MTHE: MSTHC_2338
MHOR: MSHOH_3031
MPY: Mpsy_1440
MBN: Mboo_0864
RCI: RCIX2012(hgdC-2)
LOKI: Lokiarch_29240(hgdC_2)
 » show all
Reference
1  [PMID:8365476]
  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
FEBS Lett 329:329-31 (1993)
DOI:10.1016/0014-5793(93)80247-r
  Sequence
Reference
2  [PMID:7607244]
  Authors
Muller U, Buckel W
  Title
Activation of (R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans.
  Journal
Eur J Biochem 230:698-704 (1995)
DOI:10.1111/j.1432-1033.1995.0698h.x
  Sequence
Reference
3  [PMID:11243821]
  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
J Mol Biol 307:297-308 (2001)
DOI:10.1006/jmbi.2000.4496
  Sequence
Reference
4  [PMID:11967068]
  Authors
Dickert S, Pierik AJ, Buckel W
  Title
Molecular characterization of phenyllactate dehydratase and its initiator from Clostridium sporogenes.
  Journal
Mol Microbiol 44:49-60 (2002)
DOI:10.1046/j.1365-2958.2002.02867.x
  Sequence
Reference
5  [PMID:12610725]
  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
Arch Microbiol 179:197-204 (2003)
DOI:10.1007/s00203-003-0517-8
Reference
6  [PMID:15374661]
  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
FEMS Microbiol Rev 28:455-68 (2004)
DOI:10.1016/j.femsre.2004.03.001
Reference
7  [PMID:15654892]
  Authors
Kim J, Darley D, Buckel W
  Title
2-Hydroxyisocaproyl-CoA dehydratase and its activator from Clostridium difficile.
  Journal
FEBS J 272:550-61 (2005)
DOI:10.1111/j.1742-4658.2004.04498.x
  Sequence
Reference
8  [PMID:18337824]
  Authors
Kim J, Darley DJ, Buckel W, Pierik AJ
  Title
An allylic ketyl radical intermediate in clostridial amino-acid fermentation.
  Journal
Nature 452:239-42 (2008)
DOI:10.1038/nature06637
Reference
9  [PMID:22827463]
  Authors
Knauer SH, Buckel W, Dobbek H
  Title
On the ATP-dependent activation of the radical enzyme (R)-2-hydroxyisocaproyl-CoA dehydratase.
  Journal
Biochemistry 51:6609-22 (2012)
DOI:10.1021/bi300571z
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 5.6.1.9
IUBMB Enzyme Nomenclature: 5.6.1.9
ExPASy - ENZYME nomenclature database: 5.6.1.9
BRENDA, the Enzyme Database: 5.6.1.9

DBGET integrated database retrieval system