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Overview for MACiE Entry M0116

Version history

General Information

EC Number: 1.6.1.2 (A member of the Oxidoreductases, Acting on NADH or NADPH, With NAD+ or NADP+ as acceptor)

Enzyme Name: NAD(P)+ transhydrogenase (AB-specific)

Biological Species: Rhodospirillum rubrum (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

  • Q2RSB2 - NAD(P) transhydrogenase subunit alpha part 1
  • Q2RSB4 - NAD(P) transhydrogenase subunit beta

Representative PDB Code: 1hzz - THE ASYMMETRIC COMPLEX OF THE TWO NUCLEOTIDE-BINDINGCOMPONENTS (DI, DIII) OF PROTON-TRANSLOCATINGTRANSHYDROGENASE (Resolution = 2.50 Å).

Catalytic CATH Codes:

"Other" CATH Codes:

Display structure information

Overall Reaction:

Image of NADP

Image of NADH

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Image of NADPH

Image of NAD

NADP
C00006
CHEBI:18009
NADH
C00004
CHEBI:16908
NADPH
C00005
CHEBI:16474
NAD
C00003
CHEBI:15846

Overall Comment: This enzyme couples the transfer of reducing equivalents (hydride-ion equivalents) between NAD(H) and NADP(H) to inward proton translocation across mitochondrial and bacterial membranes. The coupling reactions occur within the protein by long distance conformational changes of the reducing equivalents.


View similar reactions


Stepwise Description of the Reaction

Step 1Asp132C obtains a proton, causing a rearrangement of the active site.
Step 2NAD eliminates a hydride ion, which adds to NADP.
Step 3Asp132C releases its proton.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Arg 127 A Side Chain
Asp 135 A Side Chain
Tyr 235 A Side Chain
Asp 132 C Side Chain

References

  1. D. J. Rodrigues et al. (2001), Eur. J. Biochem., 268, 1430-1438. A change in ionization of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase regulates both hydride transfer and nucleotide release.
    Medline: 11231296
  2. G. I. van Boxel et al. (2003), Biochemistry, 42, 1217-1226. Glutamine 132 in the NAD(H)-binding component of proton-translocating transhydrogenase tethers the nucleotides before hydride transfer.
    Medline: 12564924
  3. O. C. Mather et al. (2004), Biochemistry, 43, 10952-10964. Differential inhibition of six copper amine oxidases by a family of 4-(aryloxy)-2-butynamines: evidence for a new mode of inactivation.
    Medline: 15323556
  4. A. Singh et al. (2003), J. Biol. Chem., 278, 33208-33216. Interactions between transhydrogenase and thio-nicotinamide Analogues of NAD(H) and NADP(H) underline the importance of nucleotide conformational changes in coupling to proton translocation.
    Medline: 12791694

Homologue information for M0116 (1hzz)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)



Entries with at least one Catalytic CATH code in common (different mechanisms):

MACiE Entry Enzyme Name
EC Number
PDB code CATH code Composite
Reaction Similarity
Catalytic Machinery
Similarity
M0255 alcohol dehydrogenase
1.1.1.1
1mg5 3.40.50.720
0.20.142Compare
M0092 UDP-glucose 6-dehydrogenase
1.1.1.22
1dli 3.40.50.720
0.29030.18Compare
M0021 malate dehydrogenase (oxaloacetate-decarboxylating)
1.1.1.38
1do8 3.40.50.720
0.33330.5311Compare
M0227 GDP-L-fucose synthase
1.1.1.271
1e6u 3.40.50.720
0.250.0898Compare
M0067 alanine dehydrogenase
1.4.1.1
1pjb 3.40.50.1770
0.21420.0999Compare
M0110 D-amino-acid oxidase
1.4.3.3
1c0p 3.40.50.720
0.23330Compare
M0237 pteridine reductase
1.5.1.33
2c7v 3.40.50.720
0.35590.72Compare
M0142 ferredoxin-NADP+ reductase
1.18.1.2
1e6e 3.40.50.720
0.12120.225Compare
M0090 adenosylhomocysteinase
3.3.1.1
1b3r 3.40.50.720
0.36660.2653Compare
M0240 histone/protein deacetylase
3.5.1.-
1szd 3.40.50.1220
0.20830.4684Compare
M0226 UDP-sulfoquinovose synthase
3.13.1.1
1qrr 3.40.50.720
0.4150.09Compare
M0220 benzoylformate decarboxylase
4.1.1.7
1mcz 3.40.50.1220
0.30550Compare
M0228 dTDP-glucose 4,6-dehydratase
4.2.1.46
1bxk 3.40.50.720
0.3870.3592Compare
M0188 UDP-glucose 4-epimerase
5.1.3.2
1xel 3.40.50.720
0.50.1125Compare

View a comparison of the other reactions in MACiE with the CATH domain 3.40.50.1220

View a comparison of the other reactions in MACiE with the CATH domain 3.40.50.720


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ
Link to EzCatDB

GOA logo
catalytic activity (molecular function)
binding (molecular function)
plasma membrane (cellular component)
metabolic process (biological process)
NAD(P)+ transhydrogenase activity (molecular function)
NAD(P)+ transhydrogenase (AB-specific) activity (molecular function)
membrane (cellular component)
integral component of membrane (cellular component)
oxidoreductase activity (molecular function)
NADP binding (molecular function)
oxidation-reduction process (biological process)
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