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Q53WH9

- ACDH_THET8

UniProt

Q53WH9 - ACDH_THET8

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Protein

Acetaldehyde dehydrogenase

Gene
TTHB247
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of acetaldehyde or propanal to acetyl-CoA or propanoyl-CoA, respectively, using NAD+ and coenzyme A. The aldehyde substrates can be directly channeled from the aldolase TTHB246 to the dehydrogenase TTHB247. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds.1 Publication

Catalytic activityi

Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH.1 Publication
Propanal + CoA + NAD+ = propanoyl-CoA + NADH.1 Publication

Kineticsi

The catalytic efficiency is similar when using acetaldehyde or propanaldehyde as substrate.

  1. KM=5.5 mM for acetaldehyde (at pH 8 and 25 degrees Celsius)1 Publication
  2. KM=6.4 mM for propanaldehyde (at pH 8 and 25 degrees Celsius)
  3. KM=15.4 mM for acetaldehyde (when TTHB247 is in complex with the aldolase TTHB246, at pH 8 and 25 degrees Celsius)
  4. KM=16.1 mM for propanaldehyde (when TTHB247 is in complex with the aldolase TTHB246, at pH 8 and 25 degrees Celsius)

Temperature dependencei

Has a half-life of only 1.6 hours at 50 degrees Celsius. When TTHB247 is in complex with TTHB246, its half-life is increased by approximately 4 hours.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei127 – 1271Acyl-thioester intermediate By similarity
Binding sitei278 – 2781NAD By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 154NAD By similarity
Nucleotide bindingi158 – 1669NAD By similarity

GO - Molecular functioni

  1. acetaldehyde dehydrogenase (acetylating) activity Source: UniProtKB-HAMAP
  2. NAD binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. aromatic compound catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-2270-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetaldehyde dehydrogenase (EC:1.2.1.10)
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating]
Propanal dehydrogenase (CoA-propanoylating) (EC:1.2.1.87)
Propanaldehyde dehydrogenase
Gene namesi
Ordered Locus Names:TTHB247
Encoded oniPlasmid pTT270 Publication
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Plasmid pTT27

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 307307Acetaldehyde dehydrogenaseUniRule annotationPRO_0000387749Add
BLAST

Interactioni

Subunit structurei

Monomer. Can also form a heterotetramer composed of two aldolase (TTHB246) and two dehydrogenase (TTHB247) subunits. Upon complex formation, the aldolase shows a 5-fold increase in substrate affinity, while the dehydrogenase shows a 3-fold decrease; the kcat values of each enzyme are reduced by 2-fold when they are in a complex.1 Publication

Protein-protein interaction databases

STRINGi300852.TTHB247.

Structurei

3D structure databases

ProteinModelPortaliQ53WH9.
SMRiQ53WH9. Positions 1-299.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG4569.
HOGENOMiHOG000052149.
KOiK04073.
OMAiHQGNVNM.
OrthoDBiEOG6H1PXH.
PhylomeDBiQ53WH9.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01657. Ac_ald_DH_ac.
InterProiIPR003361. Acetaldehyde_dehydrogenase.
IPR015426. Acetylaldehyde_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view]
PfamiPF09290. AcetDehyd-dimer. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF015689. Actaldh_dh_actl. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03215. ac_ald_DH_ac. 1 hit.

Sequencei

Sequence statusi: Complete.

Q53WH9-1 [UniParc]FASTAAdd to Basket

« Hide

MSERVKVAIL GSGNIGTDLM YKLLKNPGHM ELVAVVGIDP KSEGLARARA    50
LGLEASHEGI AYILERPEIK IVFDATSAKA HVRHAKLLRE AGKIAIDLTP 100
AARGPYVVPP VNLKEHLDKD NVNLITCGGQ ATIPLVYAVH RVAPVLYAEM 150
VSTVASRSAG PGTRQNIDEF TFTTARGLEA IGGAKKGKAI IILNPAEPPI 200
LMTNTVRCIP EDEGFDREAV VASVRAMERE VQAYVPGYRL KADPVFERLP 250
TPWGERTVVS MLLEVEGAGD YLPKYAGNLD IMTASARRVG EVFAQHLLGK 300
PVEEVVA 307
Length:307
Mass (Da):33,115
Last modified:May 24, 2005 - v1
Checksum:i7778943730EC4177
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008227 Genomic DNA. Translation: BAD72043.1.
RefSeqiYP_145486.1. NC_006462.1.

Genome annotation databases

EnsemblBacteriaiBAD72043; BAD72043; BAD72043.
GeneIDi3169218.
KEGGittj:TTHB247.
PATRICi23959444. VBITheThe93045_2203.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008227 Genomic DNA. Translation: BAD72043.1 .
RefSeqi YP_145486.1. NC_006462.1.

3D structure databases

ProteinModelPortali Q53WH9.
SMRi Q53WH9. Positions 1-299.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300852.TTHB247.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD72043 ; BAD72043 ; BAD72043 .
GeneIDi 3169218.
KEGGi ttj:TTHB247.
PATRICi 23959444. VBITheThe93045_2203.

Phylogenomic databases

eggNOGi COG4569.
HOGENOMi HOG000052149.
KOi K04073.
OMAi HQGNVNM.
OrthoDBi EOG6H1PXH.
PhylomeDBi Q53WH9.

Enzyme and pathway databases

BioCyci TTHE300852:GH8R-2270-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_01657. Ac_ald_DH_ac.
InterProi IPR003361. Acetaldehyde_dehydrogenase.
IPR015426. Acetylaldehyde_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view ]
Pfami PF09290. AcetDehyd-dimer. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF015689. Actaldh_dh_actl. 1 hit.
SMARTi SM00859. Semialdhyde_dh. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR03215. ac_ald_DH_ac. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  2. "Protein-protein interactions and substrate channeling in orthologous and chimeric aldolase-dehydrogenase complexes."
    Baker P., Hillis C., Carere J., Seah S.Y.
    Biochemistry 51:1942-1952(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, COMPLEX WITH TTHB246, ALDEHYDE CHANNELING.
    Strain: HB8 / ATCC 27634 / DSM 579.

Entry informationi

Entry nameiACDH_THET8
AccessioniPrimary (citable) accession number: Q53WH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: May 24, 2005
Last modified: July 9, 2014
This is version 60 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

Complete proteome, Plasmid, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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