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UniProtKB - P80175 (ADHN_AMYME)
Protein
NDMA-dependent alcohol dehydrogenase
Gene
N/A
Organism
Amycolatopsis methanolica
Status
Functioni
Catalytically different from common alcohol dehydrogenases. Effective in oxidizing ethanol, other primary alcohols and benzylalcohol only in the presence of p-nitroso-N,N-dimethylaniline (NDMA) as an electron acceptor. NADH acts as a cofactor here instead as a coenzyme.
1 PublicationCatalytic activityi
- EC:1.1.99.361 Publication
Cofactori
NADH1 Publication
Activity regulationi
Inhibited by trans-4-(N,N-dimethylamino)-cinnamaldehyde through direct binding to the catalytic zinc ion in a substrate-like geometry. Isobutyramide acts as competitive inhibitor with respect to the electron acceptor NDMA. Acetaldehyde, AMP, ADP, ATP, as well as CuSO4, FeSO4, HgCl2, NiCl2, ZnSO4, KCN, and NaN3 are additional inhibitors of the catalytic activity.3 Publications
Kineticsi
KM for benzylalcohol is lower than 0.005 mM.1 Publication
- KM=0.082 mM for ethanol1 Publication
- KM=0.0039 mM for 1-propanol1 Publication
- KM=0.0025 mM for 1-butanol1 Publication
- KM=13.4 mM for 2-propanol1 Publication
- KM=10.1 mM for 2-butanol1 Publication
- KM=6.0 mM for formaldehyde1 Publication
- Vmax=5.9 µmol/min/mg enzyme toward ethanol1 Publication
- Vmax=6.09 µmol/min/mg enzyme toward 1-propanol1 Publication
- Vmax=6.09 µmol/min/mg enzyme toward 1-butanol1 Publication
- Vmax=5.94 µmol/min/mg enzyme toward 2-propanol1 Publication
- Vmax=5.7 µmol/min/mg enzyme toward 2-butanol1 Publication
- Vmax=5.7 µmol/min/mg enzyme toward benzylalcohol1 Publication
- Vmax=4.96 µmol/min/mg enzyme toward formaldehyde1 Publication
pH dependencei
Optimum pH is 7.1 Publication
Temperature dependencei
Optimum temperature is 45 degrees Celsius.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 40 | Zinc 1; catalyticBy similarity | 1 | |
Metal bindingi | 61 | Zinc 1; catalyticBy similarity | 1 | |
Metal bindingi | 91 | Zinc 2By similarity | 1 | |
Metal bindingi | 94 | Zinc 2By similarity | 1 | |
Metal bindingi | 97 | Zinc 2By similarity | 1 | |
Metal bindingi | 105 | Zinc 2By similarity | 1 | |
Metal bindingi | 167 | Zinc 1; catalyticBy similarity | 1 |
GO - Molecular functioni
- oxidoreductase activity Source: UniProtKB-KW
- zinc ion binding Source: InterPro
Keywordsi
Molecular function | Oxidoreductase |
Ligand | Metal-binding, NAD, Zinc |
Enzyme and pathway databases
BRENDAi | 1.1.99.36, 314 |
Names & Taxonomyi
Protein namesi | Recommended name: NDMA-dependent alcohol dehydrogenase1 Publication (EC:1.1.99.361 Publication)Short name: NDMA-ADH1 Publication Alternative name(s): Nicotinoprotein alcohol/aldehyde oxidoreductase1 Publication |
Organismi | Amycolatopsis methanolica |
Taxonomic identifieri | 1814 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Pseudonocardiales › Pseudonocardiaceae › Amycolatopsis |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000064453 | 1 – 371 | NDMA-dependent alcohol dehydrogenaseAdd BLAST | 371 |
Interactioni
Subunit structurei
Homotrimer.
1 PublicationFamily & Domainsi
Sequence similaritiesi
Belongs to the zinc-containing alcohol dehydrogenase family.Curated
Family and domain databases
InterProi | View protein in InterPro IPR013149, ADH_C IPR013154, ADH_N IPR023921, ADH_Zn_actinomycetes IPR002328, ADH_Zn_CS IPR011032, GroES-like_sf IPR036291, NAD(P)-bd_dom_sf IPR020843, PKS_ER |
Pfami | View protein in Pfam PF08240, ADH_N, 1 hit PF00107, ADH_zinc_N, 1 hit |
SMARTi | View protein in SMART SM00829, PKS_ER, 1 hit |
SUPFAMi | SSF50129, SSF50129, 2 hits SSF51735, SSF51735, 1 hit |
TIGRFAMsi | TIGR03989, Rxyl_3153, 1 hit |
PROSITEi | View protein in PROSITE PS00059, ADH_ZINC, 1 hit |
i Sequence
Sequence statusi: Complete.
P80175-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKTKAAVLHS AGKPFEIEEL ELDGPREGEV LIKYTAAGLC HSDLHLIDND
60 70 80 90 100
LVPRFPIVGG HEGAGVIEDV GPGVTKVKPG DHVVCSFIPN CGTCRYCATG
110 120 130 140 150
RSNLCDMGAT ILDGGMPDGS FRFHRGGTDY GAMCMLGTFS ERATISQHSV
160 170 180 190 200
VKVDDWLPLE TAVLVGCGVP TGWASANYAG GVRAGDTCVV YGIGGIGINA
210 220 230 240 250
VQGAAHAGAA NVIAVDPVAF KREKALELGA THAFASADEA AAKVAELTWG
260 270 280 290 300
QMADQALITV GTVVEQVVTD AFNVIGKGGT VVITGLANPE KLTVHLSGGV
310 320 330 340 350
MTLFEKTVKG TLFGSANPQY DIVRLLRLYQ AGHVKLDELV TKRYSLEEVN
360 370
EGYQDLRDGK NIRGVIMHSA D
Sequence databases
PIRi | S30335 |
Similar proteinsi
Cross-referencesi
Sequence databases
PIRi | S30335 |
3D structure databases
SMRi | P80175 |
ModBasei | Search... |
Enzyme and pathway databases
BRENDAi | 1.1.99.36, 314 |
Family and domain databases
InterProi | View protein in InterPro IPR013149, ADH_C IPR013154, ADH_N IPR023921, ADH_Zn_actinomycetes IPR002328, ADH_Zn_CS IPR011032, GroES-like_sf IPR036291, NAD(P)-bd_dom_sf IPR020843, PKS_ER |
Pfami | View protein in Pfam PF08240, ADH_N, 1 hit PF00107, ADH_zinc_N, 1 hit |
SMARTi | View protein in SMART SM00829, PKS_ER, 1 hit |
SUPFAMi | SSF50129, SSF50129, 2 hits SSF51735, SSF51735, 1 hit |
TIGRFAMsi | TIGR03989, Rxyl_3153, 1 hit |
PROSITEi | View protein in PROSITE PS00059, ADH_ZINC, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ADHN_AMYME | |
Accessioni | P80175Primary (citable) accession number: P80175 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1993 |
Last sequence update: | October 16, 2013 | |
Last modified: | February 23, 2022 | |
This is version 74 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencingDocuments
- SIMILARITY comments
Index of protein domains and families