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Escherichia coli K-12 substr. MG1655 Transporter: pyridine nucleotide transhydrogenase

Synonyms: PntAB

Subunit composition of pyridine nucleotide transhydrogenase = [PntB]2[PntA]2
         pyridine nucleotide transhydrogenase, β subunit = PntB (summary available)
         pyridine nucleotide transhydrogenase, α subunit = PntA (summary available)

Summary:
E. coli PntAB is a membrane bound proton translocating pyridine nucleotide transhydrogenase which couples the reversible reduction of NADP by NADH to an inward proton translocation across the membrane [Clarke85a, Clarke85]. The activity of PntAB is a major source of cytosolic NADPH in E. coli [Sauer04a].

The functional enzyme assembles as a tetramer composed of two alpha and two beta subunits [Hou90]. The enzyme complex contains three domains: domains 1 and 3 protrude from the membrane and contain the binding sites for NAD(H) and NADP(H) respectively [Johansson05] and domain 2 which spans the membrane. The transmembrane domain consists of 13 α-helices (4 from the α subunit and 9 from the β subunit) [Meuller99]. Mutagenesis of the βhis91 residue reduces proton translocation in vitro [Holmberg94, Glavas95].

E. coli also contains an energy independent soluble pyridine nucleotide transhydrogenase encoded by the sthA gene. Its primary physiological role appears to be the reoxidation of NADPH [Canonaco01, Sauer04a]. The two transhydrogenases are also distinguished by the stereospecificity of the reducing equivalents transfer. SthA is a BB-specific transhydrogenase, while PntAB is AB-specific.

Transcription of pntA is downregulated by growth on acetate [Sauer04a].

Reviews: [Bizouarn00, Rydstrom98, Pedersen08, Bizouarn02]

Citations: [Ahmad92, Ahmad92a, Clarke86, Bragg96, Yamaguchi03, Bergkvist00, Johansson02, Hou01, Glavas95a, Bragg00, Pedersen03, Hanson79a, Hanson79, Hanson80]

Locations: inner membrane

Molecular Weight: 217.0 kD (experimental) [Hou90 ]

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006740 - NADPH regeneration Inferred from experiment [Sauer04a]
Molecular Function: GO:0008750 - NAD(P)+ transhydrogenase (AB-specific) activity Inferred from experiment [Clarke85, Hoek74]
Cellular Component: GO:0005887 - integral component of plasma membrane Inferred from experiment [Clarke85]
GO:0005886 - plasma membrane [Clarke85a]

Credits:
Last-Curated ? 28-Jun-2011 by Mackie A , Macquarie University


Enzymatic reaction of: pyridine nucleotide transhydrogenase

Synonyms: transhydrogenase, NAD(P)(+) transhydrogenase (AB-specific), nicotinamide nucleotide transhydrogenase, NADPH:NAD+ oxidoreductase (AB-specific)

Alternative Substrates for NADH: reduced 3-acetylpyridine adenine dinucleotide [Clarke85 ]

In Pathways: NAD phosphorylation and dephosphorylation I

Summary:
Dissociation constants for the physiological nucleotide substrates and products have been measured and are as follows: NADPH, 0.87 µM; NADP+, 16 µM; NADH, 50 µM; and NAD+, 100-500 µM [Bizouarn05].

Inhibitors (Irreversible): 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole [Bragg99]

Inhibitors (Unknown Mechanism): dicyclohexylcarbodiimide [Clarke85, Glavas93]

Kinetic Parameters:

Substrate
Km (μM)
Citations
NADH
1.7, 2.0
[Meuller97, BRENDA14]
NADH
3.0, 19.0, 63.0
[Hu95, BRENDA14]
NADPH
14.0
[Hanson79a, BRENDA14]
NADPH
5.1, 15.0
[Meuller97, BRENDA14]
NADPH
23.0, 29.0
[Clarke85, BRENDA14]

pH(opt): 5.5 [BRENDA14, Hu95], 6.5 [BRENDA14, Egorov04]


Subunit of pyridine nucleotide transhydrogenase: pyridine nucleotide transhydrogenase, β subunit

Synonyms: PntB

Gene: pntB Accession Numbers: EG10745 (EcoCyc), b1602, ECK1597

Locations: inner membrane

Sequence Length: 462 AAs

Molecular Weight: 48.723 kD (from nucleotide sequence)

Molecular Weight: 47.0 kD (experimental) [Clarke85]

pI: 6.09

GO Terms:

Biological Process: GO:0006740 - NADPH regeneration Inferred from experiment [Sauer04a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Johansson05, vanBoxel03, Cotton01]
GO:0008746 - NAD(P)+ transhydrogenase activity Inferred from experiment [Clarke85a]
GO:0008750 - NAD(P)+ transhydrogenase (AB-specific) activity Inferred from experiment Inferred by computational analysis [GOA01a, GOA01, Hoek74]
GO:0050661 - NADP binding Inferred from experiment Inferred by computational analysis [GOA01, Bergkvist00]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, DiazMejia09, Zhang07, Daley05, LopezCampistrou05, Clarke85a]
GO:0005887 - integral component of plasma membrane Inferred from experiment [Clarke85a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11, GOA01]

MultiFun Terms: cell structure membrane
metabolism central intermediary metabolism unassigned reversible reactions
transport Transporters of Unknown Classification

Unification Links: EcoliWiki:b1602 , ModBase:P0AB67 , PR:PRO_000023563 , Pride:P0AB67 , Protein Model Portal:P0AB67 , RefSeq:NP_416119 , SMR:P0AB67 , String:511145.b1602 , Swiss-Model:P0AB67 , UniProt:P0AB67

Relationship Links: InterPro:IN-FAMILY:IPR012136 , PDB:Structure:2BRU , Pfam:IN-FAMILY:PF02233

Summary:
PntB is an inner membrane protein with nine predicted transmembrane domains. The C terminus is located in the cytoplasm [Daley05] and contains the NADP(H) binding site [Johansson99, Bergkvist00].

Essentiality data for pntB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Subunit of pyridine nucleotide transhydrogenase: pyridine nucleotide transhydrogenase, α subunit

Synonyms: PntA

Gene: pntA Accession Numbers: EG10744 (EcoCyc), b1603, ECK1598

Locations: inner membrane

Sequence Length: 510 AAs

Molecular Weight: 54.623 kD (from nucleotide sequence)

Molecular Weight: 50.0 kD (experimental) [Clarke85]

pI: 5.88

GO Terms:

Biological Process: GO:0006740 - NADPH regeneration Inferred from experiment [Johansson05, Sauer04a]
GO:0015992 - proton transport Inferred by computational analysis [GOA01]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Johansson05]
GO:0008750 - NAD(P)+ transhydrogenase (AB-specific) activity Inferred from experiment Inferred by computational analysis [GOA01a, Johansson05, Clarke85a, Hoek74]
GO:0046983 - protein dimerization activity Inferred from experiment [Johansson05]
GO:0051287 - NAD binding Inferred from experiment [Johansson05]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11]
GO:0008746 - NAD(P)+ transhydrogenase activity Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11, GOA01]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, DiazMejia09, Zhang07, Daley05, Clarke85a]
GO:0005887 - integral component of plasma membrane Inferred from experiment [Meuller99, Clarke85a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11]

MultiFun Terms: cell structure membrane
metabolism central intermediary metabolism unassigned reversible reactions
transport Transporters of Unknown Classification

Unification Links: DIP:DIP-366N , EcoliWiki:b1603 , Mint:MINT-1299705 , ModBase:P07001 , PR:PRO_000023562 , Pride:P07001 , Protein Model Portal:P07001 , RefSeq:NP_416120 , SMR:P07001 , String:511145.b1603 , UniProt:P07001

Relationship Links: InterPro:IN-FAMILY:IPR007698 , InterPro:IN-FAMILY:IPR007886 , InterPro:IN-FAMILY:IPR008142 , InterPro:IN-FAMILY:IPR008143 , InterPro:IN-FAMILY:IPR024605 , InterPro:IN-FAMILY:IPR026255 , PDB:Structure:1X13 , PDB:Structure:1X14 , PDB:Structure:1X15 , PDB:Structure:2BRU , Pfam:IN-FAMILY:PF01262 , Pfam:IN-FAMILY:PF05222 , Pfam:IN-FAMILY:PF12769 , Prosite:IN-FAMILY:PS00836 , Prosite:IN-FAMILY:PS00837 , Smart:IN-FAMILY:SM01002 , Smart:IN-FAMILY:SM01003

Summary:
PntA is the α subunit of the membrane bound proton translocating pyridine nucleotide transhydrogenase. It contains the NADP(H) binding site [Johansson05].

Essentiality data for pntA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

References

Ahmad92: Ahmad S, Glavas NA, Bragg PD (1992). "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." Eur J Biochem 1992;207(2);733-9. PMID: 1633824

Ahmad92a: Ahmad S, Glavas NA, Bragg PD (1992). "Subunit interactions involved in the assembly of pyridine nucleotide transhydrogenase in the membranes of Escherichia coli." J Biol Chem 1992;267(10);7007-12. PMID: 1551908

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bergkvist00: Bergkvist A, Johansson C, Johansson T, Rydstrom J, Karlsson BG (2000). "Interactions of the NADP(H)-binding domain III of proton-translocating transhydrogenase from escherichia coli with NADP(H) and the NAD(H)-binding domain I studied by NMR and site-directed mutagenesis." Biochemistry 39(41);12595-605. PMID: 11027139

Bizouarn00: Bizouarn T, Fjellstrom O, Meuller J, Axelsson M, Bergkvist A, Johansson C, Goran Karlsson B, Rydstrom J (2000). "Proton translocating nicotinamide nucleotide transhydrogenase from E. coli. Mechanism of action deduced from its structural and catalytic properties." Biochim Biophys Acta 1457(3);211-28. PMID: 10773166

Bizouarn02: Bizouarn T, Althage M, Pedersen A, Tigerstrom A, Karlsson J, Johansson C, Rydstrom J (2002). "The organization of the membrane domain and its interaction with the NADP(H)-binding site in proton-translocating transhydrogenase from E. coli." Biochim Biophys Acta 1555(1-3);122-7. PMID: 12206903

Bizouarn05: Bizouarn T, van Boxel GI, Bhakta T, Jackson JB (2005). "Nucleotide binding affinities of the intact proton-translocating transhydrogenase from Escherichia coli." Biochim Biophys Acta 1708(3);404-10. PMID: 15935988

Bragg00: Bragg PD, Hou C (2000). "Crosslinking between alpha and beta subunits defines the orientation and spatial relationship of some of the transmembrane helices of the proton-translocating pyridine nucleotide transhydrogenase of Escherichia coli." Biochem Biophys Res Commun 273(3);955-9. PMID: 10891354

Bragg96: Bragg PD, Hou C (1996). "The role of conserved histidine residues in the pyridine nucleotide transhydrogenase of Escherichia coli." Eur J Biochem 241(2);611-8. PMID: 8917463

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BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Canonaco01: Canonaco F, Hess TA, Heri S, Wang T, Szyperski T, Sauer U (2001). "Metabolic flux response to phosphoglucose isomerase knock-out in Escherichia coli and impact of overexpression of the soluble transhydrogenase UdhA." FEMS Microbiol Lett 204(2);247-52. PMID: 11731130

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Clarke86: Clarke DM, Loo TW, Gillam S, Bragg PD (1986). "Nucleotide sequence of the pntA and pntB genes encoding the pyridine nucleotide transhydrogenase of Escherichia coli." Eur J Biochem 1986;158(3);647-53. PMID: 3525165

Cotton01: Cotton NP, White SA, Peake SJ, McSweeney S, Jackson JB (2001). "The crystal structure of an asymmetric complex of the two nucleotide binding components of proton-translocating transhydrogenase." Structure 9(2);165-76. PMID: 11250201

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Egorov04: Egorov MV, Tigerstrom A, Pestov NB, Korneenko TV, Kostina MB, Shakhparonov MI, Rydstrom J (2004). "Purification of a recombinant membrane protein tagged with a calmodulin-binding domain: properties of chimeras of the Escherichia coli nicotinamide nucleotide transhydrogenase and the C-terminus of human plasma membrane Ca2+ -ATPase." Protein Expr Purif 36(1);31-9. PMID: 15177281

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

Glavas93: Glavas N, Ahmad S, Bragg PD, Olausson T, Rydstrom J (1993). "Identification of N,N'-dicyclohexylcarbodiimide-reactive glutamic and aspartic acid residues in Escherichia coli transhydrogenase and the exchange of these by site-specific mutagenesis." J Biol Chem 1993;268(19);14125-30. PMID: 8100227

Glavas95: Glavas NA, Hou C, Bragg PD (1995). "Involvement of histidine-91 of the beta subunit in proton translocation by the pyridine nucleotide transhydrogenase of Escherichia coli." Biochemistry 34(23);7694-702. PMID: 7779816

Glavas95a: Glavas NA, Bragg PD (1995). "Evidence for the presence of two pyridine nucleotide-binding sites on the beta subunit of the Escherichia coli pyridine nucleotide transhydrogenase." Biochem Mol Biol Int 35(2);297-306. PMID: 7663384

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

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Hanson80: Hanson RL, Rose C (1980). "Effects of an insertion mutation in a locus affecting pyridine nucleotide transhydrogenase (pnt::Tn5) on the growth of Escherichia coli." J Bacteriol 141(1);401-4. PMID: 6986364

Hoek74: Hoek JB, Rydstrom J, Hojeberg B (1974). "Comparative studies on nicotinamide nucleotide transhydrogenase from different sources." Biochim Biophys Acta 333(2);237-45. PMID: 19400036

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Pedersen03: Pedersen A, Karlsson J, Althage M, Rydstrom J (2003). "Properties of the apo-form of the NADP(H)-binding domain III of proton-pumping Escherichia coli transhydrogenase: implications for the reaction mechanism of the intact enzyme." Biochim Biophys Acta 1604(2);55-9. PMID: 12765762

Pedersen08: Pedersen A, Karlsson GB, Rydstrom J (2008). "Proton-translocating transhydrogenase: an update of unsolved and controversial issues." J Bioenerg Biomembr 40(5);463-73. PMID: 18972197

Rydstrom98: Rydstrom J, Hu X, Fjellstrom O, Meuller J, Zhang J, Johansson C, Bizouarn T (1998). "Domains, specific residues and conformational states involved in hydride ion transfer and proton pumping by nicotinamide nucleotide transhydrogenase from Escherichia coli." Biochim Biophys Acta 1365(1-2);10-6. PMID: 9693716

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UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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