ACDH_PSEUF
ID ACDH_PSEUF Reviewed; 312 AA.
AC Q52060;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Acetaldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01657};
DE EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657};
DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] {ECO:0000255|HAMAP-Rule:MF_01657};
GN Name=dmpF;
OS Pseudomonas sp. (strain CF600).
OG Plasmid pVI150.
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=79676;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=CF600;
RX PubMed=1732207; DOI=10.1128/jb.174.3.711-724.1992;
RA Shingler V., Marklund U., Powlowski J.;
RT "Nucleotide sequence and functional analysis of the complete phenol/3,4-
RT dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600.";
RL J. Bacteriol. 174:711-724(1992).
RN [2]
RP PROTEIN SEQUENCE OF 1-6, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP ACTIVITY REGULATION, SUBUNIT, INTERACTION WITH DMPG, AND PH DEPENDENCE.
RC STRAIN=CF600;
RX PubMed=8419288; DOI=10.1128/jb.175.2.377-385.1993;
RA Powlowski J., Sahlman L., Shingler V.;
RT "Purification and properties of the physically associated meta-cleavage
RT pathway enzymes 4-hydroxy-2-ketovalerate aldolase and aldehyde
RT dehydrogenase (acylating) from Pseudomonas sp. strain CF600.";
RL J. Bacteriol. 175:377-385(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH DMPG AND NAD,
RP SUBUNIT, AND REACTION MECHANISM.
RC STRAIN=CF600;
RX PubMed=12764229; DOI=10.1073/pnas.1236794100;
RA Manjasetty B.A., Powlowski J., Vrielink A.;
RT "Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a
RT reactive and volatile intermediate.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:6992-6997(2003).
CC -!- FUNCTION: Catalyzes the conversion of acetaldehyde to acetyl-CoA, using
CC NAD(+) and coenzyme A. Can also act on propanal and butanal to form
CC propanoyl-CoA and butanoyl-CoA, respectively. Is the final enzyme in
CC the meta-cleavage pathway for the degradation of aromatic compounds
CC such as phenols, cresols and catechols. NADP(+) can replace NAD(+) but
CC the rate of reaction is much slower. {ECO:0000269|PubMed:1732207}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01657, ECO:0000269|PubMed:8419288};
CC -!- ACTIVITY REGULATION: Is not activated by Mn(2+), Mg(2+), Ca(2+), Zn(2+)
CC or Co(2+). {ECO:0000269|PubMed:8419288}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Activity increases gradually over the pH range 6.5-8.5.
CC {ECO:0000269|PubMed:8419288};
CC -!- PATHWAY: Aromatic compound metabolism; phenol degradation.
CC -!- SUBUNIT: Heterotetramer composed of two DmpG (aldolase) and two DmpF
CC (dehydrogenase) subunits, which allows a direct channeling of
CC acetaldehyde between the two active sites.
CC {ECO:0000269|PubMed:12764229, ECO:0000269|PubMed:8419288}.
CC -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01657, ECO:0000305}.
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DR EMBL; X60835; CAA43226.1; -; Genomic_DNA.
DR PIR; S24419; S24419.
DR PDB; 1NVM; X-ray; 1.70 A; B/D/F/H=1-312.
DR PDBsum; 1NVM; -.
DR AlphaFoldDB; Q52060; -.
DR SMR; Q52060; -.
DR IntAct; Q52060; 1.
DR KEGG; ag:CAA43226; -.
DR BioCyc; MetaCyc:MON-12780; -.
DR BRENDA; 1.2.1.10; 5085.
DR UniPathway; UPA00728; -.
DR EvolutionaryTrace; Q52060; -.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR GO; GO:0019439; P:aromatic compound catabolic process; IDA:UniProtKB.
DR GO; GO:0019336; P:phenol-containing compound catabolic process; IEA:UniProtKB-UniPathway.
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 3D-structure; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW NAD; Oxidoreductase; Plasmid.
FT CHAIN 1..312
FT /note="Acetaldehyde dehydrogenase"
FT /id="PRO_0000404201"
FT ACT_SITE 132
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 ECO:0000269|PubMed:12764229"
FT BINDING 163..171
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657,
FT ECO:0000269|PubMed:12764229"
FT BINDING 290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657,
FT ECO:0000269|PubMed:12764229"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:1NVM"
FT TURN 118..123
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 132..145
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 150..160
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 190..199
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 207..217
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 220..235
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1NVM"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 268..277
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 289..310
FT /evidence="ECO:0007829|PDB:1NVM"
SQ SEQUENCE 312 AA; 32685 MW; 2B38A98CE97B50DC CRC64;
MNQKLKVAII GSGNIGTDLM IKVLRNAKYL EMGAMVGIDA ASDGLARAQR MGVTTTYAGV
EGLIKLPEFA DIDFVFDATS ASAHVQNEAL LRQAKPGIRL IDLTPAAIGP YCVPVVNLEE
HLGKLNVNMV TCGGQATIPM VAAVSRVAKV HYAEIVASIS SKSAGPGTRA NIDEFTETTS
KAIEVIGGAA KGKAIIIMNP AEPPLIMRDT VYVLSAAADQ AAVAASVAEM VQAVQAYVPG
YRLKQQVQFD VIPESAPLNI PGLGRFSGLK TSVFLEVEGA AHYLPAYAGN LDIMTSAALA
TAERMAQSML NA
