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Q79AF6

- ACDH4_BURXL

UniProt

Q79AF6 - ACDH4_BURXL

Protein

Acetaldehyde dehydrogenase 4

Gene

bphJ

Organism
Burkholderia xenovorans (strain LB400)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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

    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.
    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

    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: October 1, 2014
    This is version 73 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