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Protein

(S)-1-Phenylethanol dehydrogenase

Gene

ped

Organism
Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1))
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NAD-dependent stereospecific oxidation of (S)-1-phenylethanol to acetophenone in the degradation of ethylbenzene.2 Publications

Catalytic activityi

(S)-1-phenylethanol + NAD+ = acetophenone + NADH.2 Publications

Kineticsi

  1. KM=1.6 µM for (S)-1-phenylethanol1 Publication
  2. KM=51 µM for NAD+1 Publication
  3. KM=1 µM for acetophenone1 Publication
  4. KM=3.3 µM for NADH+1 Publication
  1. Vmax=1.4 µmol/min/mg enzyme with (S)-1-phenylethanol as substrate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381NAD1 Publication
Binding sitei89 – 891NAD; via carbonyl oxygen1 Publication
Binding sitei93 – 931NAD1 Publication
Binding sitei141 – 1411SubstrateBy similarity
Active sitei154 – 1541Proton acceptor
Binding sitei158 – 1581NAD1 Publication
Binding sitei191 – 1911NAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 193NAD1 Publication
Nucleotide bindingi61 – 633NAD1 Publication
Nucleotide bindingi184 – 1874NAD1 Publication

GO - Molecular functioni

GO - Biological processi

  • anaerobic ethylbenzene catabolic process Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, Nucleotide-binding

Enzyme and pathway databases

BioCyciAARO76114:GJTA-1323-MONOMER.
MetaCyc:MONOMER-1364.
BRENDAi1.1.1.311. 604.

Names & Taxonomyi

Protein namesi
Recommended name:
(S)-1-Phenylethanol dehydrogenase (EC:1.1.1.311)
Gene namesi
Name:ped
Ordered Locus Names:AZOSEA13030
ORF Names:c1A58
OrganismiAromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1))
Taxonomic identifieri76114 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAromatoleum
Proteomesi
  • UP000006552 Componenti: Chromosome

Pathology & Biotechi

Biotechnological usei

The reverse reaction is of biotechnological interest for the specific production of chiral alcohols from ketones.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 249248(S)-1-Phenylethanol dehydrogenasePRO_0000418749Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi76114.c1A58.

Structurei

Secondary structure

1
249
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 74Combined sources
Beta strandi9 – 135Combined sources
Turni14 – 163Combined sources
Helixi18 – 2912Combined sources
Beta strandi33 – 408Combined sources
Helixi43 – 519Combined sources
Beta strandi56 – 605Combined sources
Helixi66 – 8015Combined sources
Beta strandi85 – 884Combined sources
Helixi98 – 1003Combined sources
Helixi103 – 11311Combined sources
Helixi115 – 13117Combined sources
Beta strandi134 – 1396Combined sources
Helixi142 – 1454Combined sources
Helixi152 – 17221Combined sources
Helixi173 – 1753Combined sources
Beta strandi177 – 1848Combined sources
Helixi196 – 2027Combined sources
Beta strandi209 – 2113Combined sources
Helixi218 – 22710Combined sources
Helixi230 – 2323Combined sources
Beta strandi239 – 2457Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EW8X-ray2.10A/B/C/D1-249[»]
2EWMX-ray2.40A/B1-249[»]
ProteinModelPortaliQ5P5I4.
SMRiQ5P5I4. Positions 3-249.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5P5I4.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108KEZ. Bacteria.
ENOG410XRY7. LUCA.
KOiK14746.
OrthoDBiEOG6N3CR8.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5P5I4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQRLKDKLA VITGGANGIG RAIAERFAVE GADIAIADLV PAPEAEAAIR
60 70 80 90 100
NLGRRVLTVK CDVSQPGDVE AFGKQVISTF GRCDILVNNA GIYPLIPFDE
110 120 130 140 150
LTFEQWKKTF EINVDSGFLM AKAFVPGMKR NGWGRIINLT STTYWLKIEA
160 170 180 190 200
YTHYISTKAA NIGFTRALAS DLGKDGITVN AIAPSLVRTA TTEASALSAM
210 220 230 240
FDVLPNMLQA IPRLQVPLDL TGAAAFLASD DASFITGQTL AVDGGMVRH
Length:249
Mass (Da):26,662
Last modified:January 4, 2005 - v1
Checksum:i2CA2967B5B6B32C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR555306 Genomic DNA. Translation: CAI07428.1.
RefSeqiWP_011237148.1. NC_006513.1.

Genome annotation databases

EnsemblBacteriaiCAI07428; CAI07428; c1A58.
KEGGieba:c1A58.
PATRICi20968729. VBIAroAro98752_1324.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR555306 Genomic DNA. Translation: CAI07428.1.
RefSeqiWP_011237148.1. NC_006513.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EW8X-ray2.10A/B/C/D1-249[»]
2EWMX-ray2.40A/B1-249[»]
ProteinModelPortaliQ5P5I4.
SMRiQ5P5I4. Positions 3-249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi76114.c1A58.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAI07428; CAI07428; c1A58.
KEGGieba:c1A58.
PATRICi20968729. VBIAroAro98752_1324.

Phylogenomic databases

eggNOGiENOG4108KEZ. Bacteria.
ENOG410XRY7. LUCA.
KOiK14746.
OrthoDBiEOG6N3CR8.

Enzyme and pathway databases

BioCyciAARO76114:GJTA-1323-MONOMER.
MetaCyc:MONOMER-1364.
BRENDAi1.1.1.311. 604.

Miscellaneous databases

EvolutionaryTraceiQ5P5I4.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
    Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
    Arch. Microbiol. 183:27-36(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: EbN1.
  2. "(S)-1-phenylethanol dehydrogenase of Azoarcus sp. strain EbN1, an enzyme of anaerobic ethylbenzene catabolism."
    Kniemeyer O., Heider J.
    Arch. Microbiol. 176:129-135(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-27, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: EbN1.
  3. "Crystal structure and enzyme kinetics of the (S)-specific 1-phenylethanol dehydrogenase of the denitrifying bacterium strain EbN1."
    Hoffken H.W., Duong M., Friedrich T., Breuer M., Hauer B., Reinhardt R., Rabus R., Heider J.
    Biochemistry 45:82-93(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, CATALYTIC ACTIVITY, BIOTECHNOLOGY, SUBUNIT.
    Strain: EbN1.

Entry informationi

Entry nameiPED_AROAE
AccessioniPrimary (citable) accession number: Q5P5I4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: January 4, 2005
Last modified: May 11, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.