Summary: NAD(P) transhydrogenase beta subunit
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This is the Wikipedia entry entitled "NAD(P)+ transhydrogenase (Re/Si-specific)". More...
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NAD(P)+ transhydrogenase (Re/Si-specific) Edit Wikipedia article
In enzymology, a NAD(P)+ transhydrogenase (AB-specific) (EC 126.96.36.199) is an enzyme that catalyzes the chemical reaction
- NADPH + NAD+ NADP+ + NADH
Thus, the two substrates of this enzyme are NADPH and NAD+, whereas its two products are NADP+ and NADH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is NADPH:NAD+ oxidoreductase (AB-specific). Other names in common use include pyridine nucleotide transhydrogenase, transhydrogenase, NAD(P)+ transhydrogenase, nicotinamide adenine dinucleotide (phosphate) transhydrogenase, NAD+ transhydrogenase, NADH transhydrogenase, nicotinamide nucleotide transhydrogenase, NADPH-NAD+ transhydrogenase, pyridine nucleotide transferase, NADPH-NAD+ oxidoreductase, NADH-NADP+-transhydrogenase, NADPH:NAD+ transhydrogenase, H+-Thase, energy-linked transhydrogenase, and NAD(P)+ transhydrogenase (AB-specific). This enzyme participates in nicotinate and nicotinamide metabolism.
As of late 2007, 19 structures have been solved for this class of enzymes, with PDB accession codes 1NM5, 1PNO, 1PNQ, 1PT9, 1PTJ, 1U28, 1U2D, 1U2G, 1U31, 1X13, 1X14, 1X15, 1XLT, 2BRU, 2FR8, 2FRD, 2FSV, 2OO5, and 2OOR.
- Everse, J., Anderson, B. and You, K. (Eds.), The Pyridine Nucleotide Coenzymes, The Pyridine Nucleotide Coenzymes, New York, 1982, p. 279-324.
- You KS (1985). "Stereospecificity for nicotinamide nucleotides in enzymatic and chemical hydride transfer reactions". CRC. Crit. Rev. Biochem. 17: 313â€“451. PMIDÂ 3157549.
- The CAS registry number for this enzyme class is Template:CAS registry.
Gene Ontology (GO) codes
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NAD(P) transhydrogenase beta subunit Provide feedback
This family corresponds to the beta subunit of NADP transhydrogenase in prokaryotes, and either the protein N- or C terminal in eukaryotes. The domain is often found in conjunction with PF01262. Pyridine nucleotide transhydrogenase catalyses the reduction of NAD+ to NADPH. A complete loss of activity occurs upon mutation of Gly314 in E. coli .
Ahmad S, Glavas NA, Bragg PD; , Eur J Biochem 1992;207:733-739.: A mutation at Gly314 of the beta subunit of the Escherichia coli pyridine nucleotide transhydrogenase abolishes activity and affects the NADP(H)-induced conformational change. PUBMED:1633824 EPMC:1633824
Internal database links
|Similarity to PfamA using HHSearch:||TPP_enzyme_M|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR034300
NAD(P) transhydrogenase catalyses the transfer of reducing equivalents between NAD(H) and NADP(H), coupled to the translocation of protons across a membrane [ PUBMED:12788487 ]. It is an integral membrane protein found in most organisms except for yeasts, plants and some bacterial species. In bacterial species it is located in the cytoplasmic membrane, while in mitochondria it is located in the inner membrane. Under most physiological conditions this enzyme synthesises NADPH, driven by consumption of the proton electrochemical gradient. The resulting NADPH is subsequently used for biosynthetic reactions or the reduction of glutathione.
Bacterial NADP(H) transhydrogenases consist of two subunits, an alpha subunit with an NAD(H)-binding domain and a beta subunit with an NADP(H)-binding domain [ PUBMED:12974635 ]. This entry corresponds to the beta subunit of NADP transhydrogenase in prokaryotes, and either the protein N- or C-terminal domain in eukaryotes.
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This family is a member of clan FAD_DHS (CL0085), which has the following description:
The members of this family adopt a Rossmann fold, similar to CLAN:CL0063. However, the members of this family are distinguished in that the FAD/NAD cofactor is bound in the opposite direction. In this arrangement, the adenosine moiety is found bound at the second half of the fold. In addition, the conserved GxGxxG motif found in classical NADP binding Rossmann folds is absent. Finally, another distinguishing characteristic is the formation of an internal hydrogen bond in the FAD molecule .
The clan contains the following 10 members:CO_dh DS DUF4917 ETF_alpha PNTB PPS_PS SIR2 SIR2_2 TPP_enzyme_M TPP_enzyme_M_2
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Key: available, not generated, — not available.
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|Seed source:||Pfam-B_2220 (release 5.2)|
|Author:||Bateman A , Mian N|
|Number in seed:||266|
|Number in full:||5960|
|Average length of the domain:||431.9 aa|
|Average identity of full alignment:||49 %|
|Average coverage of the sequence by the domain:||72.99 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||19|
|Download:||download the raw HMM for this family|
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.