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Q79AF6

- ACDH4_BURXL

UniProt

Q79AF6 - ACDH4_BURXL

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Protein
Acetaldehyde dehydrogenase 4
Gene
bphJ, Bxeno_C1122, Bxe_C1188
Organism
Burkholderia xenovorans (strain LB400)
Status
Reviewed - 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.2 Publications
Propanal + CoA + NAD+ = propanoyl-CoA + NADH.2 Publications

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

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 – 2731NAD By similarity

Regions

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

GO - Molecular functioni

  1. NAD binding Source: UniProtKB-HAMAP
  2. acetaldehyde dehydrogenase (acetylating) activity 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 4UniRule annotation
PRO_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.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG4569.
HOGENOMiHOG000052149.
KOiK04073.
OMAiREVQKYV.
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

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:July 5, 2004 - v1
Checksum:i3E9DDD9192B7D1AF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CP000272 Genomic DNA. Translation: ABE37050.1 .
X76500 Genomic DNA. Translation: CAA54035.1 .
RefSeqi YP_556400.1. NC_007953.1.

3D structure databases

ProteinModelPortali Q79AF6.
SMRi Q79AF6. Positions 1-294.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 266265.Bxe_C1188.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABE37050 ; ABE37050 ; Bxe_C1188 .
GeneIDi 4010700.
KEGGi bxe:Bxe_C1188.
PATRICi 19343361. VBIBurXen52548_8938.

Phylogenomic databases

eggNOGi COG4569.
HOGENOMi HOG000052149.
KOi K04073.
OMAi REVQKYV.
OrthoDBi EOG6H1PXH.

Enzyme and pathway databases

UniPathwayi UPA01002 .
BioCyci BXEN266265:GJII-8840-MONOMER.
SABIO-RK Q79AF6.

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. "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: May 14, 2014
This is version 72 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

Documents

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

External Data

Dasty 3

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