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InterPro: IPR016040 NAD(P)-binding domain
Protein matches
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UniProtKB Matches: 212210 proteins |
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Accession
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IPR016040 NAD(P)-bd_dom |
Type
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Domain |
Signatures
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InterPro Relationships
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Children
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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
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Found in
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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
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Contains
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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
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GO Term annotation
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Process
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GO:0008152 metabolic process
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Function
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GO:0003824 catalytic activity
GO:0005488 binding
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InterPro annotation
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Entry Details in BioMart
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Abstract
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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]
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Structural links
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SCOP:
a.100.1.1
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a.100.1.10
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a.100.1.3
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a.100.1.4
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a.100.1.5
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a.100.1.6
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a.100.1.7
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a.100.1.8
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a.7.12.1
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b.30.5.4
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b.35.1.2
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c.111.1.1
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c.111.1.2
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c.14.1.3
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c.2.1.1
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c.2.1.11
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c.2.1.12
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c.2.1.13
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c.2.1.2
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c.2.1.3
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c.2.1.4
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c.2.1.5
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c.2.1.6
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c.2.1.7
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c.2.1.8
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c.2.1.9
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c.23.12.1
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c.23.12.3
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c.23.14.3
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c.3.1.1
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c.3.1.2
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c.3.1.5
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c.4.1.1
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c.4.1.2
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c.4.1.3
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c.5.1.1
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c.58.1.1
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c.58.1.2
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d.16.1.3
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d.16.1.7
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d.162.1.2
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d.286.1.1
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d.81.1.1
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d.81.1.2
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d.81.1.3
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d.81.1.4
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d.81.1.5
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i.12.1.1
CATH:
1.10.10.520
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1.10.1040.10
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1.10.1870.10
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1.10.285.10
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1.20.5.100
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1.20.82.10
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3.30.160.110
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3.30.1780.10
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3.30.360.10
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3.30.9.10
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3.40.192.10
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3.40.50.10280
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3.40.50.1480
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3.40.50.720
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3.50.50.60
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3.90.110.10
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3.90.180.10
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3.90.25.10
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Example proteins
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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 |
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| IPR020828 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain |
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| IPR013149 |
Alcohol dehydrogenase, zinc-binding |
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| IPR001236 |
Lactate/malate dehydrogenase |
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| IPR020829 |
Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain |
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| IPR006424 |
Glyceraldehyde-3-phosphate dehydrogenase, type I |
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| IPR001557 |
L-lactate/malate dehydrogenase |
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| IPR001732 |
UDP-glucose/GDP-mannose dehydrogenase, N-terminal |
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| IPR002198 |
Short-chain dehydrogenase/reductase SDR |
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| IPR011032 |
GroES-like |
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| IPR016040 |
NAD(P)-binding domain |
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| IPR018177 |
L-lactate dehydrogenase, active site |
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| IPR013154 |
Alcohol dehydrogenase GroES-like |
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| IPR014028 |
UDP-glucose/GDP-mannose dehydrogenase, dimerisation and substrate-binding domain |
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| IPR014027 |
UDP-glucose/GDP-mannose dehydrogenase, C-terminal |
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| IPR002085 |
Alcohol dehydrogenase superfamily, zinc-containing |
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| IPR014026 |
UDP-glucose/GDP-mannose dehydrogenase, dimerisation |
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| IPR020831 |
Glyceraldehyde 3-phosphate dehydrogenase family |
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| IPR011304 |
L-lactate dehydrogenase |
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| IPR020830 |
Glyceraldehyde 3-phosphate dehydrogenase, active site |
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| IPR017476 |
Nucleotide sugar dehydrogenase |
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| IPR002424 |
Insect alcohol dehydrogenase family |
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| IPR015955 |
Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal |
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| IPR020832 |
Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain, subgroup |
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| IPR002328 |
Alcohol dehydrogenase, zinc-containing, conserved site |
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| IPR002425 |
Insect alcohol dehydrogenase |
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| IPR008927 |
6-phosphogluconate dehydrogenase, C-terminal-like |
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| IPR000173 |
Glyceraldehyde 3-phosphate dehydrogenase subfamily |
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ModBase |
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PDB Chain |
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CATH Domain |
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SCOP Domain |
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Publications
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1.
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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
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2.
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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
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3.
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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
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4.
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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
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5.
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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
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6.
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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-#
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7.
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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
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8.
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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
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9.
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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
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10.
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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
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11.
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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
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12.
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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
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Additional Reading
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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]
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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
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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
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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]
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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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