ACDH_CHLAA
ID ACDH_CHLAA Reviewed; 305 AA.
AC A9W9U2;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Caur_1350;
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
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; CP000909; ABY34578.1; -; Genomic_DNA.
DR RefSeq; WP_012257234.1; NC_010175.1.
DR RefSeq; YP_001634967.1; NC_010175.1.
DR AlphaFoldDB; A9W9U2; -.
DR SMR; A9W9U2; -.
DR STRING; 324602.Caur_1350; -.
DR EnsemblBacteria; ABY34578; ABY34578; Caur_1350.
DR KEGG; cau:Caur_1350; -.
DR PATRIC; fig|324602.8.peg.1538; -.
DR eggNOG; COG4569; Bacteria.
DR HOGENOM; CLU_062208_0_0_0; -.
DR InParanoid; A9W9U2; -.
DR OMA; TSAYVHK; -.
DR Proteomes; UP000002008; 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; Reference proteome.
FT CHAIN 1..305
FT /note="Acetaldehyde dehydrogenase"
FT /id="PRO_0000387649"
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 305 AA; 32852 MW; 84E757C1B25C747C CRC64;
MQIDKVKVAI LGSGNIGTDL MYKLLKQPGR MELALVAGID PASEGLARAR QIGIPTATDG
IESILADPDI RIVFDATSAK AHVRHARLLR DHGRIAIDLT PAARGPYVVP PVNLGEHLEA
HNVNLITCGG QATIPLVYAV SRVTAVRYAE MVSTVASRSA GPGTRQNIDE FTFTTARGLE
AIGGAREAKA IIILNPAHPP ILMRNTIYVV PEGDFDEETV RQSVAQMVAD VQQYVPGYRL
KSLPVIEQRS TPWGERPVII MLLEVEGAGD FLPTYAGNLD IMTAAARRVG ELFAAHLLSK
LEVTV