KEGG   ENZYME: 1.12.1.3Help
Entry
EC 1.12.1.3                 Enzyme                                 

Name
hydrogen dehydrogenase (NADP+);
NADP+-linked hydrogenase;
NADP+-reducing hydrogenase;
hydrogenase (ambiguous);
hydrogenase I (ambiguous)
Class
Oxidoreductases;
Acting on hydrogen as donor;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
hydrogen:NADP+ oxidoreductase
Reaction(IUBMB)
H2 + NADP+ = H+ + NADPH [RN:R07181]
Reaction(KEGG)
Substrate
H2 [CPD:C00282];
NADP+ [CPD:C00006]
Product
H+ [CPD:C00080];
NADPH [CPD:C00005]
Comment
The protein from the bacterium Desulfovibrio fructosovorans is an iron-sulfur protein that exclusively functions as a hydrogen dehydrogenase [1], while the enzyme from the archaeon Pyrococcus furiosus is a nickel, iron, iron-sulfur protein, that is part of a heterotetrameric complex where the alpha and delta subunits function as a hydrogenase while the beta and gamma subunits function as sulfur reductase (EC 1.12.98.4, sulfhydrogenase). Different from EC 1.12.1.5, hydrogen dehydrogenase [NAD(P)+].
History
EC 1.12.1.3 created 2002, modified 2013
Orthology
K17992  NADP-reducing hydrogenase subunit HndB
K17993  sulfhydrogenase subunit alpha
K17994  sulfhydrogenase subunit delta
K18330  NADP-reducing hydrogenase subunit HndA
K18331  NADP-reducing hydrogenase subunit HndC
K18332  NADP-reducing hydrogenase subunit HndD
Genes
AVL: AvCA_04400(hoxH)
AVD: AvCA6_04400(hoxH)
ACX: Achr_4360(hoxY) Achr_4370(hoxH)
MSQ: BKP64_00955 BKP64_00960
MARA: D0851_07215 D0851_07220
MICC: AUP74_02543(hoxH) AUP74_02544(hoxY)
MII: BTJ40_11460 BTJ40_11465
MICT: FIU95_09940(hoxH) FIU95_09945(hoxY)
MHYD: GTQ55_08910 GTQ55_08915
ALG: AQULUS_13030(hoxH) AQULUS_13040(hoxY)
ASIP: AQUSIP_08270(hoxY) AQUSIP_08280(hoxH)
LPM: LP6_2497(hydA) LP6_2498
LPC: LPC_2010 LPC_2011(hydA)
FNA: OOM_1816
TNI: TVNIR_2169 TVNIR_2170(vhuG_[H])
BHO: D560_2878
BHM: D558_2856
TBD: Tbd_1263
GLO: Glov_3133
GEO: Geob_0218(bamH-1) Geob_0234(bamH-2)
PCA: Pcar_1602(hndA-3) Pcar_1603(hndB-3) Pcar_1604(hndC-3) Pcar_1605(hndD-3) Pcar_1633(hndD-2) Pcar_1634(hndC-2) Pcar_1635(hndB-2) Pcar_1636(hndA-2) Pcar_1844(hndC-1) Pcar_1845(hndB-1) Pcar_1846(hndA-1) Pcar_2708(hndC-5)
DHY: DESAM_22495(hydA)
DML: Dmul_28600(nuoF3) Dmul_34230(morB)
DAL: Dalk_2271
DAT: HRM2_01590(hydA1) HRM2_16520
SCL: sce4575(hoxH)
DAX: FDQ92_01160(nuoF)
OCA: OCAR_5286
RRF: F11_01565
MGRY: MSR1_09580(hoxH) MSR1_09590(hoxY)
MGM: Mmc1_0883
AFR: AFE_0937(hoxH) AFE_0938(hoxY)
PPY: PPE_02671
PPM: PPSC2_14245(hydA)
PPO: PPM_2865(hydA)
PPOL: X809_30635
PPOY: RE92_22455
PSAB: PSAB_11940
PRI: PRIO_3935(hydA)
CBK: CLL_A2000
CBE: Cbei_1773
CBZ: Cbs_1773
CKL: CKL_0841
CKR: CKR_0754
CPAT: CLPA_c34400(hndC)
CPAE: CPAST_c34400(hndC)
CSB: CLSA_c23760(hndD)
CSQ: CSCA_4946
HSC: HVS_11610(hndB1) HVS_12575(hndD2) HVS_12580(hndC2) HVS_12585(hndB2)
CSD: Clst_0900(fhbA) Clst_0902(fdx1) Clst_0903(fhbB) Clst_0904(fhbC)
CCEL: CCDG5_0742 CCDG5_0743(hndC) CCDG5_0744(hndD)
RTO: RTO_15320
BPRO: PMF13cell1_04623(hndD_2)
CSO: CLS_02870
BPRL: CL2_24320
HSD: SD1D_2323 SD1D_2324(hndC) SD1D_2325(hndD)
PDC: CDIF630_03615(hydA)
CDC: CD196_3129(hydA)
CDL: CDR20291_3175(hydA)
PDF: CD630DERM_33140(hydA)
CST: CLOST_0839(hydA)
STH: STH3293
HMO: HM1_1029(nuoG)
AWO: Awo_c08260(hydA2) Awo_c26970(hydA1) Awo_c26980(hydB) Awo_c26990(hydD)
OVA: OBV_29610
BPRM: CL3_28570
BPRS: CK3_02010
TTE: TTE0892 TTE0893(NuoF) TTE0894(NuoG)
TKI: TKV_c19580(hydA1) TKV_c19960(hydA2)
MTHO: MOTHE_c17260(hndD1) MOTHE_c17270(hndC1) MOTHE_c19180(hndD2)
MTHZ: MOTHA_c18090(hndD1) MOTHA_c18100(hndC1) MOTHA_c19970(hndD2)
TACI: TDSAC_1040
FMA: FMG_1155
PHAR: NCTC13077_00350(nqo1)
MED: MELS_0888
MHG: MHY_20970
MANA: MAMMFC1_00410 MAMMFC1_00827(hndD_2) MAMMFC1_00828(hndC_3) MAMMFC1_00830(hndD_3) MAMMFC1_00831(hndC_4) MAMMFC1_00940(hndD_4)
STED: SPTER_13820(hndD_1) SPTER_13950(sfrA) SPTER_14070(hndB) SPTER_14080(hndC_2) SPTER_14090(hndD_3) SPTER_39510
AIN: Acin_2259(nuoG)
PFAC: PFJ30894_00902(hndB) PFJ30894_00903(hndC) PFJ30894_00904(hndD_1)
MBJ: KQ51_00322(hndB_1) KQ51_00323(hndC_1) KQ51_00324 KQ51_00791(hndD_1) KQ51_01818(hndB_2) KQ51_01835(nuoG)
MTHN: 4412656_03554(hoxY) 4412656_03555(hoxH)
NSR: NS506_04373(hydA) NS506_04374(mvhG)
RER: RER_34040
REQ: REQ_15170
SLAU: SLA_6981
SGE: DWG14_00278(hoxY) DWG14_00279(hoxH)
SRO: Sros_4826
PDX: Psed_3296
TBI: Tbis_1858
GPA: GPA_23180
TTR: Tter_1539
OTE: Oter_1545
MIN: Minf_2390(frhG) Minf_2391(frhA)
FMR: Fuma_01323(hoxH) Fuma_01324(hoxY)
GMR: GmarT_18740(hoxY) GmarT_18750(hoxH)
KST: KSMBR1_0596(nuoF_1) KSMBR1_1330(nuoF_2) KSMBR1_3673(hoxY) KSMBR1_3674(hoxH)
PBU: L21SP3_00034(hndD_1) L21SP3_00309(hndD_2) L21SP3_00310(hndC_3)
PBP: STSP1_00009(hndD_1) STSP1_00010(hndC_1) STSP1_01250(hndD_2)
PBAS: SMSP2_01580(hndB) SMSP2_01581(hndC_2) SMSP2_01582(hndD_2) SMSP2_01657(hndD_3)
ALUS: STSP2_01432(hndB) STSP2_01433(hndC) STSP2_01434(hndD) STSP2_01452(hoxH) STSP2_01453(hoxY)
BHY: BHWA1_02502(hymC) BHWA1_02503(nuoF)
BRM: Bmur_2160
BIP: Bint_0726(hymC) Bint_0727(nuoF)
EPO: Epro_0734(hydA) Epro_0735(hydB) Epro_0736
BVU: BVU_0396
BOA: Bovatus_04980(hndA) Bovatus_04981(hndD) Bovatus_04982(hndC)
PMUC: ING2E5A_0853(hndB) ING2E5A_0854(hndC) ING2E5A_0855(hndD) ING2E5A_0856(hndA)
BLQ: L21SP5_00769(hndB) L21SP5_00770(hndC_2) L21SP5_00771(hndD_1) L21SP5_00772(hndA_2) L21SP5_00830(hndD_2)
RMR: Rmar_2590
MGOT: MgSA37_01986(hoxY) MgSA37_01987(hoxH)
CCH: Cag_0245
PROC: Ptc2401_02008(hoxY) Ptc2401_02009(hoxH)
CTS: Ctha_0344
TMA: TM0011
TPT: Tpet_0912
TRQ: TRQ2_0934
TNP: Tnap_0642
DTN: DTL3_0214 DTL3_0799(hndD3)
DTU: Dtur_0918
NIO: NITINOP_0586(hydA) NITINOP_0587(hydD)
MOX: DAMO_0854
PHO: PH1292(PH1292) PH1294(PH1294)
PAB: PAB0640(hydD-2) PAB0641(hydA-2) PAB1786 PAB1787
MCJ: MCON_3103(nuoF)
BARB: AOA66_1503(shyD) AOA66_1504(hydA)
 » show all
Taxonomy
Reference
1  [PMID:9703971]
  Authors
de Luca G, de Philip P, Rousset M, Belaich JP, Dermoun Z.
  Title
The NADP-reducing hydrogenase of Desulfovibrio fructosovorans: evidence for a native complex with hydrogen-dependent methyl-viologen-reducing activity.
  Journal
Biochem Biophys Res Commun 248:591-6 (1998)
DOI:10.1006/bbrc.1998.9022
  Sequence
Reference
2  [PMID:2538471]
  Authors
Bryant FO, Adams MW
  Title
Characterization of hydrogenase from the hyperthermophilic archaebacterium, Pyrococcus furiosus.
  Journal
J Biol Chem 264:5070-9 (1989)
  Sequence
Reference
3  [PMID:8389482]
  Authors
Ma K, Schicho RN, Kelly RM, Adams MW
  Title
Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: evidence for a sulfur-reducing hydrogenase ancestor.
  Journal
Proc Natl Acad Sci U S A 90:5341-4 (1993)
DOI:10.1073/pnas.90.11.5341
Reference
4
  Authors
Ma, K., Zhou, Z.H. and Adams, M.W.
  Title
Hydrogen production from pyruvate by enzymes purified from the hyperthermophilic archaeon, Pyrococcus furiosus: A key role for NADPH.
  Journal
FEMS Microbiol Lett 122:245-250 (1994)
Reference
5  [PMID:18156274]
  Authors
van Haaster DJ, Silva PJ, Hagedoorn PL, Jongejan JA, Hagen WR
  Title
Reinvestigation of the steady-state kinetics and physiological function of the soluble NiFe-hydrogenase I of Pyrococcus furiosus.
  Journal
J Bacteriol 190:1584-7 (2008)
DOI:10.1128/JB.01562-07
Other DBs
ExplorEnz - The Enzyme Database: 1.12.1.3
IUBMB Enzyme Nomenclature: 1.12.1.3
ExPASy - ENZYME nomenclature database: 1.12.1.3
BRENDA, the Enzyme Database: 1.12.1.3
CAS: 9027-05-8

DBGET integrated database retrieval system