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Q79AF6 (ACDH4_BURXL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:bphJ
Ordered Locus Names:Bxeno_C1122
ORF Names:Bxe_C1188
OrganismBurkholderia xenovorans (strain LB400) [Complete proteome] [HAMAP]
Taxonomic identifier266265 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length304 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.4

Catalytic activity

Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH. Ref.3 Ref.6

Propanal + CoA + NAD+ = propanoyl-CoA + NADH. Ref.3 Ref.6

Enzyme regulation

Bound pyruvate or other intermediates in the aldol addition reaction catalyzed by BphI allosterically activates BphJ reductive deacylation activity. Ref.4

Pathway

Xenobiotic degradation; polychlorinated biphenyl degradation. HAMAP-Rule MF_01657

Subunit structure

Heterotetramer composed of two BphI (aldolase) and two BphJ (dehydrogenase). Ref.3

Sequence similarities

Belongs to the acetaldehyde dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

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

KM=23.6 mM for acetaldehyde (at pH 8 and 25 degrees Celsius) Ref.3

KM=23.1 mM for propanaldehyde (at pH 8 and 25 degrees Celsius)

KM=31.7 mM for butyraldehyde (at pH 8 and 25 degrees Celsius)

KM=7.7 mM for isobutyraldehyde (at pH 8 and 25 degrees Celsius)

KM=34.8 µM for NAD+ (at pH 8 and 25 degrees Celsius)

KM=561 µM for NADP+ (at pH 8 and 25 degrees Celsius)

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical termAllosteric enzyme
Complete proteome
Gene Ontology (GO)
   Biological_processaromatic compound catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

acetaldehyde dehydrogenase (acetylating) activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 304304Acetaldehyde dehydrogenase 4 HAMAP-Rule MF_01657
PRO_0000387931

Regions

Nucleotide binding162 – 1709NAD By similarity

Sites

Active site1311Acyl-thioester intermediate Ref.6
Binding site2731NAD By similarity
Site1951Responsible for governing aldehyde substrate chain length specificity

Experimental info

Mutagenesis1311C → A or S: Loss of catalytic activity. Still able to bind NAD(+), however with much lower affinity. Ref.6
Mutagenesis1701N → A or D: Displays significant reduction in the level of allosteric activation of the aldol cleavage reaction by BphI. Ref.6
Mutagenesis1711I → 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. Ref.6
Mutagenesis1951I → 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. Ref.5 Ref.6
Mutagenesis1951I → 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. Ref.5 Ref.6
Mutagenesis1951I → L: Does not significantly reduce the channeling efficiency of the enzyme complex toward acetaldehyde or propanaldehyde. Ref.5 Ref.6
Mutagenesis1951I → 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. Ref.5 Ref.6
Mutagenesis2081D → A: 2-fold decrease in catalytic efficiency. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q79AF6 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 3E9DDD9192B7D1AF

FASTA30432,237
        10         20         30         40         50         60 
MTKKIKCALI GPGNIGTDLL AKLQRSPVLE PIWMVGIDPE SDGLKRAREM GIKTTADGVD 

        70         80         90        100        110        120 
GLIPHMQADG VQIVFDATSA YVHADNSRKV NALGALMIDL TPAAIGPFCV PTVNLKEHVG 

       130        140        150        160        170        180 
KGEMNVNMVT CGGQATIPMV AAVSRVQPVA YGEIVATVSS KSAGPGTRKN IDEFTRTTAG 

       190        200        210        220        230        240 
AVEKVGGAKK GKAIIILNPA EPPLIMRDTV HCLLESEPDQ AKITESIHAM IKEVQKYVPG 

       250        260        270        280        290        300 
YKLVNGPVFD GLRVSVYLEV EGLGDYLPKY AGNLDIMTAA AARTAEMFAE EILAGQLTLQ 


PVHA 

« Hide

References

« Hide 'large scale' references
[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]"Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome shaped for versatility."
Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J., Parnell J.J. expand/collapse author list , Ramette A., Richardson P., Seeger M., Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.
Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000272 Genomic DNA. Translation: ABE37050.1.
X76500 Genomic DNA. Translation: CAA54035.1.
RefSeqYP_556400.1. NC_007953.1.

3D structure databases

ProteinModelPortalQ79AF6.
SMRQ79AF6. Positions 1-294.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266265.Bxe_C1188.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE37050; ABE37050; Bxe_C1188.
GeneID4010700.
KEGGbxe:Bxe_C1188.
PATRIC19343361. VBIBurXen52548_8938.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4569.
HOGENOMHOG000052149.
KOK04073.
OMAQRSEWLE.
OrthoDBEOG6H1PXH.
ProtClustDBPRK08300.

Enzyme and pathway databases

BioCycBXEN266265:GJII-8840-MONOMER.
SABIO-RKQ79AF6.
UniPathwayUPA01002.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_01657. Ac_ald_DH_ac.
InterProIPR003361. Acetaldehyde_dehydrogenase.
IPR015426. Acetylaldehyde_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view]
PfamPF09290. AcetDehyd-dimer. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
[Graphical view]
PIRSFPIRSF015689. Actaldh_dh_actl. 1 hit.
SMARTSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR03215. ac_ald_DH_ac. 1 hit.
ProtoNetSearch...

Entry information

Entry nameACDH4_BURXL
AccessionPrimary (citable) accession number: Q79AF6
Secondary accession number(s): Q13FT9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways