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Q52039

- ACDH2_PSEPS

UniProt

Q52039 - ACDH2_PSEPS

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Protein

Acetaldehyde dehydrogenase 2

Gene
bphX2
Organism
Pseudomonas pseudoalcaligenes
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 sitei131 – 1311Acyl-thioester intermediate By similarity
Binding sitei273 – 2731NAD By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi162 – 1709NAD 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

Names & Taxonomyi

Protein namesi
Recommended name:
Acetaldehyde dehydrogenase 2 (EC:1.2.1.10)
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating] 2
Gene namesi
Name:bphX2
OrganismiPseudomonas pseudoalcaligenes
Taxonomic identifieri330 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonasPseudomonas oleovorans/pseudoalcaligenes group

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 304304Acetaldehyde dehydrogenase 2UniRule annotationPRO_0000387707Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ52039.
SMRiQ52039. Positions 1-294.

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.

Q52039-1 [UniParc]FASTAAdd to Basket

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MTKKIKCALI GPGNIGTDLL AKLQRSPVLE PIWMVGIDPE SDGLKRAREM    50
GIKTTADGVD GLIPHMQADG VQIVFDATSA YVHADNSRKV NALGALMIDL 100
TPAAIGPFCV PTVNLKEHVG KGEMNVNMVT CGGQATIPMV AAVSRVQPVA 150
YGEIVATVSS KSAGPGTRKN IDEFTRTTAG AVEKVGGAKK GKAIIILNPA 200
EPPLIMRDTV HCLLESEPDQ AKITESIHAM IKEVQKYVPG YKLVNGPVFD 250
GLRVSVYLEV EGLGDYLPKY AGNLDIMTAA AARTAEMFAE EILAGQLTLQ 300
PVHA 304
Length:304
Mass (Da):32,237
Last modified:November 1, 1996 - v1
Checksum:i3E9DDD9192B7D1AF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D85853 Genomic DNA. Translation: BAA12885.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D85853 Genomic DNA. Translation: BAA12885.1 .

3D structure databases

ProteinModelPortali Q52039.
SMRi Q52039. Positions 1-294.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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

  1. "Functional analyses of a variety of chimeric dioxygenases constructed from two biphenyl dioxygenases that are similar structurally but different functionally."
    Kimura N., Nishi A., Goto M., Furukawa K.
    J. Bacteriol. 179:3936-3943(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: KF707.

Entry informationi

Entry nameiACDH2_PSEPS
AccessioniPrimary (citable) accession number: Q52039
Secondary accession number(s): Q59722
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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