ACDH3_COMTE
ID ACDH3_COMTE Reviewed; 316 AA.
AC Q9S153;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Acetaldehyde dehydrogenase 3 {ECO:0000255|HAMAP-Rule:MF_01657};
DE EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657};
DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] 3 {ECO:0000255|HAMAP-Rule:MF_01657};
GN Name=mhpF;
OS Comamonas testosteroni (Pseudomonas testosteroni).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=285;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TA441;
RX PubMed=10537203; DOI=10.1099/00221287-145-10-2813;
RA Arai H., Yamamoto T., Ohishi T., Shimizu T., Nakata T., Kudo T.;
RT "Genetic organization and characteristics of the 3-(3-
RT hydroxyphenyl)propionic acid degradation pathway of Comamonas testosteroni
RT TA441.";
RL Microbiology 145:2813-2820(1999).
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};
CC -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01657}.
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DR EMBL; AB024335; BAA82883.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9S153; -.
DR SMR; Q9S153; -.
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 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; NAD; Oxidoreductase.
FT CHAIN 1..316
FT /note="Acetaldehyde dehydrogenase 3"
FT /id="PRO_0000387652"
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 BINDING 163..171
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 289
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ SEQUENCE 316 AA; 33136 MW; A107BBAF90A009EF CRC64;
MTRKLKAAII GSGNIGTDLM IKILRHGKNI EMGAMVGIDP HSDGLARASR MGVATTHEGV
EGLTRMPGFA EIDFVFDATS AGAHVKNDAF LRSLKPGIRM IDLTPAAIGP YCIPVVNGDM
HLDAPNVNMV TCGGQATIPM VAAVSRVAKV HYGEIIASIA SKSAGPGTRA NIDEFTETTS
KAIEVVGGAT KGKAIIIMNP AEPPLIMRDT VYTLSALADE AAIAASVEQM AAAVQSYVPG
YRLKQQVQFD RIDTPIRIPG VGNALTGLKT SIFLEVEGAA HYLPAYAGNL DIMTSAGLRT
AEHMAERMLA TLAVAA
