ACDH_THET8
ID ACDH_THET8 Reviewed; 307 AA.
AC Q53WH9;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Acetaldehyde dehydrogenase;
DE EC=1.2.1.10;
DE AltName: Full=Acetaldehyde dehydrogenase [acetylating];
DE AltName: Full=Propanal dehydrogenase (CoA-propanoylating);
DE EC=1.2.1.87;
DE AltName: Full=Propanaldehyde dehydrogenase;
GN OrderedLocusNames=TTHB247;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OG Plasmid pTT27.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, SUBUNIT, COMPLEX WITH TTHB246, AND ALDEHYDE CHANNELING.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=22316175; DOI=10.1021/bi201832a;
RA Baker P., Hillis C., Carere J., Seah S.Y.;
RT "Protein-protein interactions and substrate channeling in orthologous and
RT chimeric aldolase-dehydrogenase complexes.";
RL Biochemistry 51:1942-1952(2012).
CC -!- FUNCTION: Catalyzes the conversion of acetaldehyde or propanal to
CC acetyl-CoA or propanoyl-CoA, respectively, using NAD(+) and coenzyme A.
CC The aldehyde substrates can be directly channeled from the aldolase
CC TTHB246 to the dehydrogenase TTHB247. Is the final enzyme in the meta-
CC cleavage pathway for the degradation of aromatic compounds.
CC {ECO:0000269|PubMed:22316175}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetaldehyde + CoA + NAD(+) = acetyl-CoA + H(+) + NADH;
CC Xref=Rhea:RHEA:23288, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.10;
CC Evidence={ECO:0000269|PubMed:22316175};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CoA + NAD(+) + propanal = H(+) + NADH + propanoyl-CoA;
CC Xref=Rhea:RHEA:36027, ChEBI:CHEBI:15378, ChEBI:CHEBI:17153,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.87;
CC Evidence={ECO:0000269|PubMed:22316175};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.5 mM for acetaldehyde (at pH 8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:22316175};
CC KM=6.4 mM for propanaldehyde (at pH 8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:22316175};
CC KM=15.4 mM for acetaldehyde (when TTHB247 is in complex with the
CC aldolase TTHB246, at pH 8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:22316175};
CC KM=16.1 mM for propanaldehyde (when TTHB247 is in complex with the
CC aldolase TTHB246, at pH 8 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:22316175};
CC Note=The catalytic efficiency is similar when using acetaldehyde or
CC propanaldehyde as substrate.;
CC Temperature dependence:
CC Has a half-life of only 1.6 hours at 50 degrees Celsius. When TTHB247
CC is in complex with TTHB246, its half-life is increased by
CC approximately 4 hours. {ECO:0000269|PubMed:22316175};
CC -!- SUBUNIT: Monomer. Can also form a heterotetramer composed of two
CC aldolase (TTHB246) and two dehydrogenase (TTHB247) subunits. Upon
CC complex formation, the aldolase shows a 5-fold increase in substrate
CC affinity, while the dehydrogenase shows a 3-fold decrease; the kcat
CC values of each enzyme are reduced by 2-fold when they are in a complex.
CC {ECO:0000269|PubMed:22316175}.
CC -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AP008227; BAD72043.1; -; Genomic_DNA.
DR RefSeq; WP_011229062.1; NC_006462.1.
DR RefSeq; YP_145486.1; NC_006462.1.
DR AlphaFoldDB; Q53WH9; -.
DR SMR; Q53WH9; -.
DR EnsemblBacteria; BAD72043; BAD72043; BAD72043.
DR GeneID; 3169218; -.
DR KEGG; ttj:TTHB247; -.
DR PATRIC; fig|300852.9.peg.2203; -.
DR HOGENOM; CLU_062208_0_0_0; -.
DR OMA; TSAYVHK; -.
DR PhylomeDB; Q53WH9; -.
DR BRENDA; 1.2.1.10; 2305.
DR BRENDA; 1.2.1.87; 2305.
DR SABIO-RK; Q53WH9; -.
DR Proteomes; UP000000532; Plasmid pTT27.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01657; Ac_ald_DH_ac; 1.
DR InterPro; IPR003361; Acetaldehyde_dehydrogenase.
DR InterPro; IPR015426; Acetylaldehyde_DH_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR Pfam; PF09290; AcetDehyd-dimer; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR PIRSF; PIRSF015689; Actaldh_dh_actl; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03215; ac_ald_DH_ac; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; NAD; Oxidoreductase; Plasmid;
KW Reference proteome.
FT CHAIN 1..307
FT /note="Acetaldehyde dehydrogenase"
FT /id="PRO_0000387749"
FT ACT_SITE 127
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 12..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 158..166
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 278
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ SEQUENCE 307 AA; 33115 MW; 7778943730EC4177 CRC64;
MSERVKVAIL GSGNIGTDLM YKLLKNPGHM ELVAVVGIDP KSEGLARARA LGLEASHEGI
AYILERPEIK IVFDATSAKA HVRHAKLLRE AGKIAIDLTP AARGPYVVPP VNLKEHLDKD
NVNLITCGGQ ATIPLVYAVH RVAPVLYAEM VSTVASRSAG PGTRQNIDEF TFTTARGLEA
IGGAKKGKAI IILNPAEPPI LMTNTVRCIP EDEGFDREAV VASVRAMERE VQAYVPGYRL
KADPVFERLP TPWGERTVVS MLLEVEGAGD YLPKYAGNLD IMTASARRVG EVFAQHLLGK
PVEEVVA
