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
GEB: 
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)
PPD: 
DMA: 
DAT: 
DTI: 
DBR: 
CLS: 
CLB: 
CACE: 
AMT: 
CTH: 
CTX: 
CCE: 
CCL: 
ESR: 
ESU: 
CSS: 
CSD: 
Clst_0900(fhbA) Clst_0902(fdx1) Clst_0903(fhbB) Clst_0904(fhbC)
CCEL: 
RCH: 
CLE: 
CCT: 
CPY: 
CSH: 
HSD: 
DAE: 
DKU: 
TJR: 
DMI: 
DED: 
DEC: 
DRS: 
ELM: 
EAC: 
AWO: 
Awo_c26970(hydA1) Awo_c26980(hydB) Awo_c26990(hydD)
IBU: 
TTE: 
TTE0892 TTE0893(NuoF) TTE0894(NuoG)
TEX: 
THX: 
TPD: 
TIT: 
TMT: 
TBO: 
TWI: 
TEP: 
TAE: 
MTA: 
TPZ: 
CSC: 
ATE: 
COB: 
CHD: 
COW: 
CKI: 
CKN: 
CLC: 
TOC: 
TTM: 
TTO: 
TXY: 
TSH: 
CPO: 
MAS: 
NTH: 
HOR: 
HAS: 
HPK: 
AAR: 
HHL: 
PFT: 
TUR: 
MBJ: 
KQ51_00322(hndB_1) KQ51_01818(hndB_2)
ATM: 
VBL: 
TBE: 
TAZ: 
TPED: 
SCD: 
SSM: 
STA: 
STQ: 
SFC: 
SBU: 
SGP: 
SLR: 
EPO: 
TAI: 
ACO: 
TLI: 
AMO: 
BACC: 
PDI: 
PBT: 
OSP: 
RBC: 
DOI: 
TMA: 
TMM: 
TMI: 
TMW: 
TMQ: 
TMX: 
TPT: 
TRQ: 
TNA: 
TNP: 
THQ: 
THZ: 
THR: 
TLE: 
TTA: 
PHY: 
TME: 
TAF: 
FNO: 
FPE: 
FIA: 
PMO: 
MPZ: 
DTN: 
KOL: 
KPF: 
MPG: 
CEX: 
DTH: 
DTU: 
BLQ: 
PHO: 
PH1292(PH1292) PH1294(PH1294)
PAB: 
PAB0640(hydD-2) PAB0641(hydA-2) PAB1786 PAB1787
PFU: 
PFI: 
PYN: 
PYA: 
PYS: 
TKO: 
TON: 
TSI: 
TBA: 
THE: 
THA: 
THM: 
TLT: 
KCR: 
 » 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 (1998) 591-6.
  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 (1989) 5070-9.
  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 (1993) 5341-4.
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 (1994) 245-250.
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 (2008) 1584-7.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9027-05-8

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