Q79AF6 (ACDH4_BURXL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetaldehyde dehydrogenase 4
EC=1.2.1.10

Alternative name(s):
Acetaldehyde dehydrogenase [acetylating] 4

Gene names

Name:	bphJ
Ordered Locus Names:	Bxeno_C1122
ORF Names:	Bxe_C1188

Organism

Burkholderia xenovorans (strain LB400) [Complete proteome] [HAMAP]

Taxonomic identifier

266265 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia xenovorans

Protein attributes

Sequence length	304 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the conversion of acetaldehyde to acetyl-CoA, 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
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 process	Aromatic hydrocarbons catabolism
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological_process	aromatic compound catabolic process Inferred from electronic annotation. Source: HAMAP cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	NAD binding Inferred from electronic annotation. Source: HAMAP acetaldehyde dehydrogenase (acetylating) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 304	304	Acetaldehyde dehydrogenase 4 HAMAP-Rule MF_01657		PRO_0000387931
Regions
	Nucleotide binding	162 – 170	9	NAD By similarity
Sites
	Active site	131	1	Acyl-thioester intermediate Ref.6
	Binding site	273	1	NAD By similarity
	Site	195	1	Responsible for governing aldehyde substrate chain length specificity
Experimental info
	Mutagenesis	131	1	C → A or S: Loss of catalytic activity. Still able to bind NAD(+), however with much lower affinity. Ref.6
	Mutagenesis	170	1	N → A or D: Displays significant reduction in the level of allosteric activation of the aldol cleavage reaction by BphI. Ref.6
	Mutagenesis	171	1	I → 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
	Mutagenesis	195	1	I → 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
	Mutagenesis	195	1	I → 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
	Mutagenesis	195	1	I → L: Does not significantly reduce the channeling efficiency of the enzyme complex toward acetaldehyde or propanaldehyde. Ref.5 Ref.6
	Mutagenesis	195	1	I → 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
	Mutagenesis	208	1	D → A: 2-fold decrease in catalytic efficiency. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q79AF6 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 3E9DDD9192B7D1AF	FASTA	304	32,237
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
RefSeq	YP_556400.1. NC_007953.1.
3D structure databases
ProteinModelPortal	Q79AF6.
SMR	Q79AF6. Positions 1-294.
ModBase	Search...
Protein-protein interaction databases
STRING	266265.Bxe_C1188.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABE37050; ABE37050; Bxe_C1188.
GeneID	4010700.
KEGG	bxe:Bxe_C1188.
PATRIC	19343361. VBIBurXen52548_8938.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG4569.
HOGENOM	HOG000052149.
KO	K04073.
OMA	TSAYVHK.
ProtClustDB	PRK08300.
Enzyme and pathway databases
BioCyc	BXEN266265:GJII-8840-MONOMER.
SABIO-RK	Q79AF6.
UniPathway	UPA01002.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_01657. Ac_ald_DH_ac.
InterPro	IPR003361. Acetaldehyde_dehydrogenase. IPR015426. Acetylaldehyde_DH_C. IPR016040. NAD(P)-bd_dom. IPR000534. Semialdehyde_DH_NAD-bd. [Graphical view]
PANTHER	PTHR21123. PTHR21123. 1 hit.
Pfam	PF09290. AcetDehyd-dimer. 1 hit. PF01118. Semialdhyde_dh. 1 hit. [Graphical view]
PIRSF	PIRSF015689. Actaldh_dh_actl. 1 hit.
SMART	SM00859. Semialdhyde_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR03215. ac_ald_DH_ac. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ACDH4_BURXL

Accession

Primary (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:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program