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InterPro: IPR016040 NAD(P)-binding domain

Protein matchesHelp
UniProtKB
Matches:
212210 proteins
AccessionHelp IPR016040 NAD(P)-bd_dom
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR000534 Semialdehyde dehydrogenase, NAD-binding
IPR000669 Mannitol dehydrogenase, core
IPR001732 UDP-glucose/GDP-mannose dehydrogenase, N-terminal
IPR002225 3-beta hydroxysteroid dehydrogenase/isomerase
IPR003781 CoA-binding
IPR003869 Polysaccharide biosynthesis protein CapD-like
IPR005106 Aspartate/homoserine dehydrogenase, NAD-binding
IPR006096 Glutamate/phenylalanine/leucine/valine dehydrogenase, C-terminal
IPR006115 6-phosphogluconate dehydrogenase, NAD-binding
IPR006140 D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding
IPR006151 Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
IPR006176 3-hydroxyacyl-CoA dehydrogenase, NAD binding
IPR007698 Alanine dehydrogenase/PNT, C-terminal
IPR011128 NAD-dependent glycerol-3-phosphate dehydrogenase, N-terminal
IPR012302 Malic enzyme, NAD-binding
IPR013116 Acetohydroxy acid isomeroreductase, catalytic
IPR013120 Male sterility, NAD-binding
IPR013149 Alcohol dehydrogenase, zinc-binding
IPR013332 Ketopantoate reductase ApbA/PanE, N-terminal
IPR013512 1-deoxy-D-xylulose 5-phosphate reductoisomerase, N-terminal
IPR015878 S-adenosyl-L-homocysteine hydrolase, NAD binding
IPR019665 Putative oxidoreductase/dehydrogenase, Rossmann-like domain
IPR019901 Ergot alkaloid biosynthesis protein
IPR020631 Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain
IPR020828 Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain
IPR020842 Polyketide synthase/Fatty acid synthase, KR
Found in IPR000043 S-adenosyl-L-homocysteine hydrolase
IPR000173 Glyceraldehyde 3-phosphate dehydrogenase subfamily
IPR000304 Delta 1-pyrroline-5-carboxylate reductase
IPR000672 Tetrahydrofolate dehydrogenase/cyclohydrolase
IPR000846 Dihydrodipicolinate reductase
IPR001088 Glycoside hydrolase, family 4
IPR001236 Lactate/malate dehydrogenase
IPR001282 Glucose-6-phosphate dehydrogenase
IPR001509 NAD-dependent epimerase/dehydratase
IPR001557 L-lactate/malate dehydrogenase
IPR002198 Short-chain dehydrogenase/reductase SDR
IPR002347 Glucose/ribitol dehydrogenase
IPR002424 Insect alcohol dehydrogenase family
IPR002425 Insect alcohol dehydrogenase
IPR002426 Ceratitis capitata alcohol dehydrogenase
IPR002427 Alcohol dehydrogenase-related protein
IPR002587 Myo-inositol-1-phosphate synthase
IPR003099 Prephenate dehydrogenase
IPR003462 Ornithine cyclodeaminase/mu-crystallin
IPR003560 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
IPR003929 Potassium channel, calcium-activated, BK, alpha subunit
IPR004432 Polyketide-type polyunsaturated fatty acid synthase, PfaA
IPR004455 NADP oxidoreductase, coenzyme F420-dependent
IPR004627 L-threonine 3-dehydrogenase
IPR005097 Saccharopine dehydrogenase
IPR005762 UDP-N-acetylmuramoylalanine-D-glutamate ligase
IPR005886 UDP-glucose 4-epimerase
IPR005888 dTDP-glucose 4,6-dehydratase
IPR005913 dTDP-4-dehydrorhamnose reductase
IPR005979 Light-dependent protochlorophyllide reductase
IPR006036 Potassium uptake protein TrkA
IPR006139 D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain
IPR006277 Sarcosine oxidase, alpha subunit, heterotetrameric
IPR006367 Sirohaem synthase, N-terminal
IPR006368 GDP-mannose 4,6-dehydratase
IPR006393 Sepiapterin reductase
IPR006422 D-erythrose-4-phosphate dehydrogenase
IPR006424 Glyceraldehyde-3-phosphate dehydrogenase, type I
IPR006436 Glyceraldehyde-3-phosphate dehydrogenase, type II
IPR007780 Bacterial NAD-glutamate dehydrogenase
IPR008030 NmrA-like
IPR008089 Nucleotide sugar epimerase
IPR008244 Bifunctional chorismate mutase/prephenate dehydrogenase T-protein
IPR008289 Pentafunctional AroM protein
IPR008299 Prephenate dehydrogenase/arogenate dehydrogenase predicted, C-terminal regulatory region-containing
IPR008354 Glucose-fructose oxidoreductase, bacterial
IPR010062 Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase
IPR010063 Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin reductase-related
IPR010091 Thiazolinyl imide reductase
IPR010097 Malate dehydrogenase, NAD-dependent, eukaryote/gamma proteobacteria
IPR010099 Sugar nucleotide epimerase YfcH, putative
IPR010185 NADPH-dependent F420 reductase
IPR010190 Diaminopimelate dehydrogenase
IPR010420 Protein of unknown function DUF1012
IPR010429 Bacterial FdrA
IPR010945 Malate dehydrogenase, NAD/NADP
IPR011182 Aspartate dehydrogenase, NAD biosynthesis
IPR011272 Lactate dehydrogenase
IPR011273 Malate dehydrogenase, NADP-dependent, plants
IPR011274 Malate dehydrogenase, NAD-dependent, cytosolic
IPR011275 Malate dehydrogenase, NAD-dependent
IPR011283 Acetoacetyl-CoA reductase
IPR011284 3-oxoacyl-(acyl-carrier-protein) reductase
IPR011285 3-oxoacyl-(acyl-carrier-protein) reductase, putative
IPR011286 2-deoxy-D-gluconate 3-dehydrogenase
IPR011294 3-hydroxybutyrate dehydrogenase
IPR011304 L-lactate dehydrogenase
IPR011348 17beta-dehydrogenase
IPR011770 Dihydrodipicolinate reductase, bacterial/plant
IPR011859 Dihydrodipicolinate reductase, plant
IPR011912 ADP-L-glycero-D-manno-heptose-6-epimerase
IPR012066 Uroporphyrin-III C-methyltransferase, yeast
IPR012070 Arogenate/prephenate dehydrogenase, plant
IPR012115 Bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase
IPR012385 Prephenate dehydrogenase, fungal
IPR012742 Alanine dehydrogenase, archaea
IPR012799 Fatty oxidation complex, alpha subunit FadB
IPR013445 CDP-glucose 4,6-dehydratase
IPR013454 Bifunctional rhamnulose-1-phosphate aldolase/alcohol dehydrogenase
IPR013952 Protein of unknown function DUF1776, fungi
IPR014007 Acetoin reductase
IPR014058 Pteridine reductase
IPR014308 Xanthine dehydrogenase accessory protein XdhC
IPR014334 Ectoine utilization protein EutC
IPR014358 Enoyl-[acyl-carrier-protein] reductase (NADH)
IPR015845 Agropine synthesis reductase
IPR016836 Uncharacterised conserved protein UCP026396, short chain dehydrogenase, Alr5284
IPR017094 Biliverdin reductase A
IPR017619 2-hydroxycyclohexanecarboxyl-CoA dehydrogenase
IPR017701 Putative selenate reductase YgfK
IPR017711 Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase
IPR017815 Myo-inositol 1-phosphate synthase, actinobacteria
IPR017829 Hopanoid-associated sugar epimerase
IPR018075 Ubiquitin-activating enzyme, E1
IPR020626 Aspartate dehydrogenase, NAD biosynthesis, prokaryotic
IPR020831 Glyceraldehyde 3-phosphate dehydrogenase family
IPR020843 Polyketide synthase, enoylreductase
IPR020884 Glutathione-regulated potassium-efflux system protein KefB
IPR020921 Erythronate-4-phosphate dehydrogenase
Contains IPR000683 Oxidoreductase, N-terminal
IPR002204 3-hydroxyisobutyrate dehydrogenase-related, conserved site
IPR002364 Quinone oxidoreductase/zeta-crystallin, conserved site
IPR003148 Regulator of K+ conductance, N-terminal
IPR006037 Regulator of K+ conductance, C-terminal
IPR006181 D-amino acid oxidase, conserved site
IPR008143 Alanine dehydrogenase/pyridine nucleotide transhydrogenase, conserved site-2
IPR013021 Myo-inositol-1-phosphate synthase, GAPDH-like
IPR013131 Mannitol dehydrogenase, N-terminal
IPR013549 Domain of unknown function DUF1731, C-terminal
IPR015884 Malic enzyme, conserved site
IPR018074 Ubiquitin-activating enzyme, E1, active site
IPR019572 Ubiquitin-activating enzyme
IPR019796 Glucose-6-phosphate dehydrogenase, active site
IPR020082 S-adenosyl-L-homocysteine hydrolase, conserved site
IPR020830 Glyceraldehyde 3-phosphate dehydrogenase, active site
IPR020867 Tetrahydrofolate dehydrogenase/cyclohydrolase, conserved site
IPR020904 Short-chain dehydrogenase/reductase, conserved site
GO Term annotationHelp
Process GO:0008152 metabolic process
Function GO:0003824 catalytic activity
GO:0005488 binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This entry represents NAD- and NADP-binding domains with a core Rossmann-type fold, which consists of 3-layers alpha/beta/alpha, where the six beta strands are parallel in the order 321456. Many different enzymes contain an NAD/NADP-binding domain, including:

  • C-terminal domain of alcohol dehydrogenases [1]
  • Tyrosine-dependent oxidoreductases (also known as short-chain dehydrogenases) [2]
  • N-terminal domain of glyceraldehyde-3-phosphate dehydrogenase [3]
  • NAD-binding domain of formate/glycerate dehydrogenases [4]
  • N-terminal domain of sirohaem synthase [5]
  • N-terminal domain of lactate dehydrogenase [6]
  • N-terminal domain of 6-phosphogluconate dehydrogenase (the beta-sheet is extended to 8 strands) [7]
  • C-terminal domain of amino acid dehydrogenases (an extra N-terminal helix displaces the C-terminal helix [8]
  • NAD-binding domain of certain potassium channels [9]
  • C-terminal domain of the transcriptional repressor Rex [10]
  • Ornithine cyclodeaminase [11]
  • CoA-binding N-terminal domain of the alpha chain of succinyl-CoA synthetase [12]

Structural linksHelp
PDB - click here

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR016040 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O14556 Glyceraldehyde-3-phosphate dehydrogenase, testis-specific

P00330 Alcohol dehydrogenase 1

P00334 Alcohol dehydrogenase

P00342 L-lactate dehydrogenase C chain

Q19905 UDP-glucose 6-dehydrogenase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR020904 Short-chain dehydrogenase/reductase, conserved site
IPR020828 Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain
IPR013149 Alcohol dehydrogenase, zinc-binding
IPR001236 Lactate/malate dehydrogenase
IPR020829 Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain
IPR006424 Glyceraldehyde-3-phosphate dehydrogenase, type I
IPR001557 L-lactate/malate dehydrogenase
IPR001732 UDP-glucose/GDP-mannose dehydrogenase, N-terminal
IPR002198 Short-chain dehydrogenase/reductase SDR
IPR011032 GroES-like
IPR016040 NAD(P)-binding domain
IPR018177 L-lactate dehydrogenase, active site
IPR013154 Alcohol dehydrogenase GroES-like
IPR014028 UDP-glucose/GDP-mannose dehydrogenase, dimerisation and substrate-binding domain
IPR014027 UDP-glucose/GDP-mannose dehydrogenase, C-terminal
IPR002085 Alcohol dehydrogenase superfamily, zinc-containing
IPR014026 UDP-glucose/GDP-mannose dehydrogenase, dimerisation
IPR020831 Glyceraldehyde 3-phosphate dehydrogenase family
IPR011304 L-lactate dehydrogenase
IPR020830 Glyceraldehyde 3-phosphate dehydrogenase, active site
IPR017476 Nucleotide sugar dehydrogenase
IPR002424 Insect alcohol dehydrogenase family
IPR015955 Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal
IPR020832 Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain, subgroup
IPR002328 Alcohol dehydrogenase, zinc-containing, conserved site
IPR002425 Insect alcohol dehydrogenase
IPR008927 6-phosphogluconate dehydrogenase, C-terminal-like
IPR000173 Glyceraldehyde 3-phosphate dehydrogenase subfamily
ModBase
PDB Chain
CATH Domain
SCOP Domain

PublicationsHelp
1. Gibbons BJ, Hurley TD.
Structure of three class I human alcohol dehydrogenases complexed with isoenzyme specific formamide inhibitors.
Biochemistry 43 12555-62 2004 [PubMed: 15449945]
http://dx.doi.org/10.1021/bi0489107
2. Thoden JB, Hegeman AD, Wesenberg G, Chapeau MC, Frey PA, Holden HM.
Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli.
Biochemistry 36 6294-304 1997 [PubMed: 9174344]
http://dx.doi.org/10.1021/bi970025j
3. Isupov MN, Fleming TM, Dalby AR, Crowhurst GS, Bourne PC, Littlechild JA.
Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus.
J. Mol. Biol. 291 651-60 1999 [PubMed: 10448043]
http://dx.doi.org/10.1006/jmbi.1999.3003
4. Lamzin VS, Dauter Z, Popov VO, Harutyunyan EH, Wilson KS.
High resolution structures of holo and apo formate dehydrogenase.
J. Mol. Biol. 236 759-85 1994 [PubMed: 8114093]
http://dx.doi.org/10.1006/jmbi.1994.1188
5. Stroupe ME, Leech HK, Daniels DS, Warren MJ, Getzoff ED.
CysG structure reveals tetrapyrrole-binding features and novel regulation of siroheme biosynthesis.
Nat. Struct. Biol. 10 1064-73 2003 [PubMed: 14595395]
http://dx.doi.org/10.1038/nsb1007
6. Read JA, Winter VJ, Eszes CM, Sessions RB, Brady RL.
Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase.
Proteins 43 175-85 2001 [PubMed: 11276087]
http://dx.doi.org/10.1002/1097-0134(20010501)43:2<175::AID-PROT1029>3.0.CO;2-#
7. Sundaramoorthy R, Iulek J, Barrett MP, Bidet O, Ruda GF, Gilbert IH, Hunter WN.
Crystal structures of a bacterial 6-phosphogluconate dehydrogenase reveal aspects of specificity, mechanism and mode of inhibition by analogues of high-energy reaction intermediates.
FEBS J. 274 275-86 2007 [PubMed: 17222187]
http://dx.doi.org/10.1111/j.1742-4658.2006.05585.x
8. Yip KS, Stillman TJ, Britton KL, Artymiuk PJ, Baker PJ, Sedelnikova SE, Engel PC, Pasquo A, Chiaraluce R, Consalvi V.
The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures.
Structure 3 1147-58 1995 [PubMed: 8591026]
http://dx.doi.org/10.1016/S0969-2126(01)00251-9
9. Jiang Y, Pico A, Cadene M, Chait BT, MacKinnon R.
Structure of the RCK domain from the E. coli K+ channel and demonstration of its presence in the human BK channel.
Neuron 29 593-601 2001 [PubMed: 11301020]
http://dx.doi.org/10.1016/S0896-6273(01)00236-7
10. Sickmier EA, Brekasis D, Paranawithana S, Bonanno JB, Paget MS, Burley SK, Kielkopf CL.
X-ray structure of a Rex-family repressor/NADH complex insights into the mechanism of redox sensing.
Structure 13 43-54 2005 [PubMed: 15642260]
http://dx.doi.org/10.1016/j.str.2004.10.012
11. Goodman JL, Wang S, Alam S, Ruzicka FJ, Frey PA, Wedekind JE.
Ornithine cyclodeaminase: structure, mechanism of action, and implications for the mu-crystallin family.
Biochemistry 43 13883-91 2004 [PubMed: 15518536]
http://dx.doi.org/10.1021/bi048207i
12. Fraser ME, James MN, Bridger WA, Wolodko WT.
A detailed structural description of Escherichia coli succinyl-CoA synthetase.
J. Mol. Biol. 285 1633-53 1999 [PubMed: 9917402]
http://dx.doi.org/10.1006/jmbi.1998.2324

Additional ReadingHelp
Kawakami R, Sakuraba H, Goda S, Tsuge H, Ohshima T.
Refolding, characterization and crystal structure of (S)-malate dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix.
Biochim. Biophys. Acta 1794 2009 1496-504 [PubMed: 19555779]
Frayne J, Taylor A, Cameron G, Hadfield AT.
Structure of Insoluble Rat Sperm Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH) via Heterotetramer Formation with Escherichia coli GAPDH Reveals Target for Contraceptive Design.
J. Biol. Chem. 284 2009 22703-12 [PubMed: 19542219]
http://dx.doi.org/10.1074/jbc.M109.004648
Zaccai NR, Carter LG, Berrow NS, Sainsbury S, Nettleship JE, Walter TS, Harlos K, Owens RJ, Wilson KS, Stuart DI, Esnouf RM.
Crystal structure of a 3-oxoacyl-(acylcarrier protein) reductase (BA3989) from Bacillus anthracis at 2.4-A resolution.
Proteins 70 2008 562-7 [PubMed: 17894349]
http://dx.doi.org/10.1002/prot.21624
Osipiuk J, Zhou M, Moy S, Collart F, Joachimiak A.
X-Ray crystal structure of GarR-tartronate semialdehyde reductase from Salmonella typhimurium.
J. Struct. Funct. Genomics 2009 [PubMed: 19184529]
Goihberg E, Dym O, Tel-Or S, Shimon L, Frolow F, Peretz M, Burstein Y.
Thermal stabilization of the protozoan Entamoeba histolytica alcohol dehydrogenase by a single proline substitution.
Proteins 72 2008 711-9 [PubMed: 18260103]
http://dx.doi.org/10.1002/prot.21946
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InterPro 23.1