Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acetaldehyde dehydrogenase 4

Gene

bphJ

Organism
Burkholderia xenovorans (strain LB400)
Status
Reviewed-Annotation score: Annotation score: 5 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. Displays broad specificity since it can utilize aliphatic aldehydes from two to five carbons in length as substrates; the aldehyde substrates can be directly channeled from the aldolase BphI to the dehydrogenase BphJ. Is the final enzyme in the meta-cleavage pathway for the degradation of polychlorinated biphenyls (PCBs). Is also able to utilize NADP+ instead of NAD+. Is not active with succinic semialdehyde or picolinaldehyde as substrates. Can also catalyze the reverse reaction, i.e. the reductive deacylation of acetyl-CoA to acetaldehyde, which is then channeled to the BphI active site. The BphI-BphJ enzyme complex exhibits unique bidirectionality in substrate channeling and allosteric activation.2 Publications

Catalytic activityi

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

Enzyme regulationi

Bound pyruvate or other intermediates in the aldol addition reaction catalyzed by BphI allosterically activates BphJ reductive deacylation activity.1 Publication

Kineticsi

kcat is 17.2 and 16.3 sec(-1) with acetaldehyde and propanaldehyde as substrate, respectively (at pH 8 and 25 degrees Celsius).

  1. KM=23.6 mM for acetaldehyde (at pH 8 and 25 degrees Celsius)1 Publication
  2. KM=23.1 mM for propanaldehyde (at pH 8 and 25 degrees Celsius)1 Publication
  3. KM=31.7 mM for butyraldehyde (at pH 8 and 25 degrees Celsius)1 Publication
  4. KM=7.7 mM for isobutyraldehyde (at pH 8 and 25 degrees Celsius)1 Publication
  5. KM=34.8 µM for NAD+ (at pH 8 and 25 degrees Celsius)1 Publication
  6. KM=561 µM for NADP+ (at pH 8 and 25 degrees Celsius)1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei131 – 1311Acyl-thioester intermediate1 Publication
Sitei195 – 1951Responsible for governing aldehyde substrate chain length specificity
Binding sitei273 – 2731NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi162 – 1709NADBy 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, NADP

Enzyme and pathway databases

BioCyciBXEN266265:GJII-8840-MONOMER.
SABIO-RKQ79AF6.
UniPathwayiUPA01002.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetaldehyde dehydrogenase 4 (EC:1.2.1.10)
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating] 4
Propanal dehydrogenase (CoA-propanoylating) (EC:1.2.1.87)
Gene namesi
Name:bphJ
Ordered Locus Names:Bxeno_C1122
ORF Names:Bxe_C1188
OrganismiBurkholderia xenovorans (strain LB400)
Taxonomic identifieri266265 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia
ProteomesiUP000001817: Chromosome 3

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1311C → A or S: Loss of catalytic activity. Still able to bind NAD(+), however with much lower affinity. 1 Publication
Mutagenesisi170 – 1701N → A or D: Displays significant reduction in the level of allosteric activation of the aldol cleavage reaction by BphI. 1 Publication
Mutagenesisi171 – 1711I → A or F: Exhibits preferences for aldehydes similar as wild-type. Exhibits about 80% of wild-type acetaldehyde channeling efficiency. Displays significant reduction in the level of allosteric activation of the aldol cleavage reaction by BphI. 1 Publication
Mutagenesisi195 – 1951I → A: 5-fold decrease in affinity for acetaldehyde. Increase in affinity for butyraldehyde and pentaldehyde, leading to a 9- and 20-fold increase in catalytic efficiency with butyraldehyde and pentaldehyde as substrate, respectively. Exhibits 84% of wild-type acetaldehyde channeling efficiency. 2 Publications
Mutagenesisi195 – 1951I → F: 4- to 7-fold decrease in catalytic efficiency with aldehydes three to four carbons in length. Does not significantly reduce the channeling efficiency of the enzyme complex toward acetaldehyde or propanaldehyde. 2 Publications
Mutagenesisi195 – 1951I → L: Does not significantly reduce the channeling efficiency of the enzyme complex toward acetaldehyde or propanaldehyde. 2 Publications
Mutagenesisi195 – 1951I → W: 5- to 16-fold decrease in catalytic efficiency with aldehydes two to four carbons in length. Exhibits 59% of wild-type acetaldehyde channeling efficiency. 2 Publications
Mutagenesisi208 – 2081D → A: 2-fold decrease in catalytic efficiency. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 304304Acetaldehyde dehydrogenase 4PRO_0000387931Add
BLAST

Interactioni

Subunit structurei

Heterotetramer composed of two BphI (aldolase) and two BphJ (dehydrogenase).1 Publication

Protein-protein interaction databases

STRINGi266265.Bxe_C1188.

Structurei

3D structure databases

ProteinModelPortaliQ79AF6.
SMRiQ79AF6. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acetaldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG4569.
HOGENOMiHOG000052149.
KOiK18366.
OMAiQRSEWLE.
OrthoDBiEOG6H1PXH.

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.

Q79AF6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKKIKCALI GPGNIGTDLL AKLQRSPVLE PIWMVGIDPE SDGLKRAREM
60 70 80 90 100
GIKTTADGVD GLIPHMQADG VQIVFDATSA YVHADNSRKV NALGALMIDL
110 120 130 140 150
TPAAIGPFCV PTVNLKEHVG KGEMNVNMVT CGGQATIPMV AAVSRVQPVA
160 170 180 190 200
YGEIVATVSS KSAGPGTRKN IDEFTRTTAG AVEKVGGAKK GKAIIILNPA
210 220 230 240 250
EPPLIMRDTV HCLLESEPDQ AKITESIHAM IKEVQKYVPG YKLVNGPVFD
260 270 280 290 300
GLRVSVYLEV EGLGDYLPKY AGNLDIMTAA AARTAEMFAE EILAGQLTLQ

PVHA
Length:304
Mass (Da):32,237
Last modified:July 5, 2004 - v1
Checksum:i3E9DDD9192B7D1AF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000272 Genomic DNA. Translation: ABE37050.1.
X76500 Genomic DNA. Translation: CAA54035.1.
RefSeqiYP_556400.1. NC_007953.1.

Genome annotation databases

EnsemblBacteriaiABE37050; ABE37050; Bxe_C1188.
GeneIDi4010700.
KEGGibxe:Bxe_C1188.
PATRICi19343361. VBIBurXen52548_8938.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000272 Genomic DNA. Translation: ABE37050.1.
X76500 Genomic DNA. Translation: CAA54035.1.
RefSeqiYP_556400.1. NC_007953.1.

3D structure databases

ProteinModelPortaliQ79AF6.
SMRiQ79AF6. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi266265.Bxe_C1188.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE37050; ABE37050; Bxe_C1188.
GeneIDi4010700.
KEGGibxe:Bxe_C1188.
PATRICi19343361. VBIBurXen52548_8938.

Phylogenomic databases

eggNOGiCOG4569.
HOGENOMiHOG000052149.
KOiK18366.
OMAiQRSEWLE.
OrthoDBiEOG6H1PXH.

Enzyme and pathway databases

UniPathwayiUPA01002.
BioCyciBXEN266265:GJII-8840-MONOMER.
SABIO-RKQ79AF6.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The biphenyl/polychlorinated biphenyl-degradation locus (bph) of Pseudomonas sp. LB400 encodes four additional metabolic enzymes."
    Hofer B., Backhaus S., Timmis K.N.
    Gene 144:9-16(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LB400.
  3. "Characterization of an aldolase-dehydrogenase complex that exhibits substrate channeling in the polychlorinated biphenyls degradation pathway."
    Baker P., Pan D., Carere J., Rossi A., Wang W., Seah S.Y.K.
    Biochemistry 48:6551-6558(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COMPLEX WITH BPHI.
  4. "Comparison of two metal-dependent pyruvate aldolases related by convergent evolution: substrate specificity, kinetic mechanism, and substrate channeling."
    Wang W., Baker P., Seah S.Y.
    Biochemistry 49:3774-3782(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  5. "Investigating the molecular determinants for substrate channeling in BphI-BphJ, an aldolase-dehydrogenase complex from the polychlorinated biphenyls degradation pathway."
    Carere J., Baker P., Seah S.Y.
    Biochemistry 50:8407-8416(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ILE-195, ALDEHYDE CHANNELING MECHANISM.
    Strain: LB400.
  6. "Substrate specificity, substrate channeling, and allostery in BphJ: an acylating aldehyde dehydrogenase associated with the pyruvate aldolase BphI."
    Baker P., Carere J., Seah S.Y.
    Biochemistry 51:4558-4567(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVE SITE, REACTION MECHANISM, MUTAGENESIS OF CYS-131; ASN-170; ILE-171; ILE-195 AND ASP-208.
    Strain: LB400.

Entry informationi

Entry nameiACDH4_BURXL
AccessioniPrimary (citable) accession number: Q79AF6
Secondary accession number(s): Q13FT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: July 5, 2004
Last modified: January 7, 2015
This is version 75 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

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.