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Q9S153

- ACDH3_COMTE

UniProt

Q9S153 - ACDH3_COMTE

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Protein
Acetaldehyde dehydrogenase 3
Gene
mhpF
Organism
Comamonas testosteroni (Pseudomonas testosteroni)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD+ and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds By similarity.UniRule annotation

Catalytic activityi

Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei132 – 1321Acyl-thioester intermediate By similarity
Binding sitei289 – 2891NAD By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 154NAD By similarity
Nucleotide bindingi163 – 1719NAD By similarity

GO - Molecular functioni

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

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

Names & Taxonomyi

Protein namesi
Recommended name:
Acetaldehyde dehydrogenase 3 (EC:1.2.1.10)
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating] 3
Gene namesi
Name:mhpF
OrganismiComamonas testosteroni (Pseudomonas testosteroni)
Taxonomic identifieri285 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Acetaldehyde dehydrogenase 3UniRule annotation
PRO_0000387652Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ9S153.
SMRiQ9S153. Positions 1-309.

Family & Domainsi

Sequence similaritiesi

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.

Q9S153-1 [UniParc]FASTAAdd to Basket

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MTRKLKAAII GSGNIGTDLM IKILRHGKNI EMGAMVGIDP HSDGLARASR    50
MGVATTHEGV EGLTRMPGFA EIDFVFDATS AGAHVKNDAF LRSLKPGIRM 100
IDLTPAAIGP YCIPVVNGDM HLDAPNVNMV TCGGQATIPM VAAVSRVAKV 150
HYGEIIASIA SKSAGPGTRA NIDEFTETTS KAIEVVGGAT KGKAIIIMNP 200
AEPPLIMRDT VYTLSALADE AAIAASVEQM AAAVQSYVPG YRLKQQVQFD 250
RIDTPIRIPG VGNALTGLKT SIFLEVEGAA HYLPAYAGNL DIMTSAGLRT 300
AEHMAERMLA TLAVAA 316
Length:316
Mass (Da):33,136
Last modified:May 1, 2000 - v1
Checksum:iA107BBAF90A009EF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB024335 Genomic DNA. Translation: BAA82883.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB024335 Genomic DNA. Translation: BAA82883.1 .

3D structure databases

ProteinModelPortali Q9S153.
SMRi Q9S153. Positions 1-309.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...