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ACDH_CHLAD
ID   ACDH_CHLAD              Reviewed;         303 AA.
AC   B8GBV4;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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   OrderedLocusNames=Cagg_2033;
OS   Chloroflexus aggregans (strain MD-66 / DSM 9485).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=326427;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-66 / DSM 9485;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chloroflexus aggregans DSM 9485.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001337; ACL24921.1; -; Genomic_DNA.
DR   RefSeq; WP_015940780.1; NC_011831.1.
DR   AlphaFoldDB; B8GBV4; -.
DR   SMR; B8GBV4; -.
DR   STRING; 326427.Cagg_2033; -.
DR   EnsemblBacteria; ACL24921; ACL24921; Cagg_2033.
DR   KEGG; cag:Cagg_2033; -.
DR   eggNOG; COG4569; Bacteria.
DR   HOGENOM; CLU_062208_0_0_0; -.
DR   OMA; TSAYVHK; -.
DR   OrthoDB; 1432332at2; -.
DR   Proteomes; UP000002508; Chromosome.
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..303
FT                   /note="Acetaldehyde dehydrogenase"
FT                   /id="PRO_0000387647"
FT   ACT_SITE        128
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         13..16
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         159..167
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   303 AA;  32590 MW;  11E1AECD4BC07C6B CRC64;
     MQADKVKVAI LGSGNIGTDL MYKLLRQPGP MELALVAGID PASEGLARAR QLGIPTSASG
     IEAILADPEI RIVFDATSAK AHVRHARLLR EHGRIAIDLT PAARGPYVVP PVNLGMHLDA
     PNVNLITCGG QATIPLVYAV SRVTPVRYAE MVSTVSSRSA GPGTRQNIDE FTFTTARGLE
     VIGGAHQAKA IIILNPANPP ILMRNTIYVL PEGEFDETAV QNSVAQMVAD VQQYVPGYRL
     KNRPVIERRA TPWGERPVLI MLLEVEGAGD FLPRYAGNLD IMTSAARRVG EVFAQHILKE
     VAA
 
 
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