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Protein

Alcohol dehydrogenase

Gene

adh

Organism
Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Multifunctional alcohol dehydrogenase exhibiting NAD+-dependent dehydrogenase activities for 2,3-butanediol, ethanol and acetaldehyde, and reductase activities for acetoin (NADH-dependent), and diacetyl and acetaldehyde (independently of whether NADH or NADPH is the reductant). The rate of oxidation of 2,3-butanediol is much higher than for the oxidation of ethanol. Has acetaldehyde dehydrogenase activity leading to acetate formation. May function in the release of excess reducing power in the absence of exogenous hydrogen acceptors such as oxygen.By similarity

Catalytic activityi

An alcohol + NAD+ = an aldehyde or ketone + NADH.By similarity
(R,R)-butane-2,3-diol + NAD+ = (R)-acetoin + NADH.By similarity
An aldehyde + NAD+ + H2O = a carboxylate + NADH.By similarity

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi41Zinc; catalyticBy similarity1
Metal bindingi62Zinc; catalyticBy similarity1
Metal bindingi63Zinc; catalyticBy similarity1
Metal bindingi167Zinc; catalyticBy similarity1

GO - Molecular functioni

Keywordsi

Molecular functionOxidoreductase
LigandMetal-binding, NAD, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase (EC:1.1.1.1By similarity, EC:1.1.1.4By similarity, EC:1.2.1.3By similarity)
Gene namesi
Name:adh
OrganismiCupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha)
Taxonomic identifieri106590 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001607472 – 366Alcohol dehydrogenaseAdd BLAST365

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi381666.H16_A0757.

Structurei

3D structure databases

ProteinModelPortaliP14940.
SMRiP14940.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CPQ. Bacteria.
COG1063. LUCA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiView protein in InterPro
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
PfamiView protein in Pfam
PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
SMARTiView protein in SMART
SM00829. PKS_ER. 1 hit.
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
PROSITEiView protein in PROSITE
PS00059. ADH_ZINC. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14940-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAMMKAAVF VEPGRIELAD KPIPDIGPND ALVRITTTTI CGTDVHILKG
60 70 80 90 100
EYPVAKGLTV GHEPVGIIEK LGSAVTGYRE GQRVIAGAIC PNFNSYAAQD
110 120 130 140 150
GVASQDGSYL MASGQCGCHG YKATAGWRFG NMIDGTQAEY VLVPDAQANL
160 170 180 190 200
TPIPDGLTDE QVLMCPDIMS TGFKGAENAN IRIGHTVAVF AQGPIGLCAT
210 220 230 240 250
AGARLCGATT IIAIDGNDHR LEIARKMGAD VVLNFRNCDV VDEVMKLTGG
260 270 280 290 300
RGVDASIEAL GTQATFEQSL RVLKPGGTLS SLGVYSSDLT IPLSAFAAGL
310 320 330 340 350
GDHKINTALC PGGKERMRRL INVIESGRVD LGALVTHQYR LDDIVAAYDL
360
FANQRDGVLK IAIKPH
Length:366
Mass (Da):38,566
Last modified:April 1, 1990 - v1
Checksum:i6F531C8D7FEA874B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03362 Genomic DNA. Translation: AAA21953.1.
PIRiA30196.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03362 Genomic DNA. Translation: AAA21953.1.
PIRiA30196.

3D structure databases

ProteinModelPortaliP14940.
SMRiP14940.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi381666.H16_A0757.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CPQ. Bacteria.
COG1063. LUCA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiView protein in InterPro
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
PfamiView protein in Pfam
PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
SMARTiView protein in SMART
SM00829. PKS_ER. 1 hit.
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
PROSITEiView protein in PROSITE
PS00059. ADH_ZINC. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiADH_CUPNE
AccessioniPrimary (citable) accession number: P14940
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: March 15, 2017
This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.