ADHE_CLOAB
ID ADHE_CLOAB Reviewed; 862 AA.
AC P33744; Q45808; Q45809;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Aldehyde-alcohol dehydrogenase {ECO:0000303|PubMed:8300540};
DE Short=AAD {ECO:0000303|PubMed:8300540};
DE Includes:
DE RecName: Full=Alcohol dehydrogenase {ECO:0000303|PubMed:8300540};
DE Short=ADH {ECO:0000303|PubMed:8300540};
DE EC=1.1.1.1 {ECO:0000269|PubMed:8300540};
DE Includes:
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000303|PubMed:8300540};
DE Short=ALDH {ECO:0000303|PubMed:8300540};
DE EC=1.2.1.3 {ECO:0000269|PubMed:8300540};
GN Name=adhE {ECO:0000303|PubMed:8226639};
GN Synonyms=aad {ECO:0000303|PubMed:8300540}; OrderedLocusNames=CA_P0162;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OG Plasmid pSOL1.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=8226639; DOI=10.1128/jb.175.21.6959-6969.1993;
RA Fischer R.J., Helms J., Duerre P.;
RT "Cloning, sequencing, and molecular analysis of the sol operon of
RT Clostridium acetobutylicum, a chromosomal locus involved in
RT solventogenesis.";
RL J. Bacteriol. 175:6959-6969(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP INDUCTION.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=8300540; DOI=10.1128/jb.176.3.871-885.1994;
RA Nair R.V., Bennett G.N., Papoutsakis E.T.;
RT "Molecular characterization of an aldehyde/alcohol dehydrogenase gene from
RT Clostridium acetobutylicum ATCC 824.";
RL J. Bacteriol. 176:871-885(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
CC -!- FUNCTION: Has both aldehyde and alcohol dehydrogenase activities. Can
CC use acetaldehyde, butyraldehyde, butanol and ethanol.
CC {ECO:0000269|PubMed:8300540}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000269|PubMed:8300540};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000269|PubMed:8300540};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence={ECO:0000269|PubMed:8300540};
CC -!- INDUCTION: Induced during switch to solvent production.
CC {ECO:0000269|PubMed:8300540}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aldehyde
CC dehydrogenase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the iron-containing
CC alcohol dehydrogenase family. {ECO:0000305}.
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DR EMBL; X72831; CAA51344.1; -; Genomic_DNA.
DR EMBL; L14817; AAD04638.1; -; Genomic_DNA.
DR EMBL; AE001438; AAK76907.1; -; Genomic_DNA.
DR PIR; A49346; A49346.
DR RefSeq; NP_149325.1; NC_001988.2.
DR RefSeq; WP_010890846.1; NC_001988.2.
DR AlphaFoldDB; P33744; -.
DR SMR; P33744; -.
DR EnsemblBacteria; AAK76907; AAK76907; CA_P0162.
DR GeneID; 45000387; -.
DR KEGG; cac:CA_P0162; -.
DR PATRIC; fig|272562.8.peg.163; -.
DR HOGENOM; CLU_007207_1_1_9; -.
DR OMA; QWFKVPP; -.
DR OrthoDB; 1456634at2; -.
DR BioCyc; MetaCyc:AADCLOS-MON; -.
DR Proteomes; UP000000814; Plasmid pSOL1.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:InterPro.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:CACAO.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006066; P:alcohol metabolic process; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR CDD; cd08178; AAD_C; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR034789; AAD_C.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012079; Bifunc_Ald-ADH.
DR PANTHER; PTHR11496; PTHR11496; 1.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PIRSF; PIRSF000111; ALDH_ADH; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
PE 1: Evidence at protein level;
KW Multifunctional enzyme; NAD; Oxidoreductase; Plasmid; Reference proteome.
FT CHAIN 1..862
FT /note="Aldehyde-alcohol dehydrogenase"
FT /id="PRO_0000087839"
FT ACT_SITE 244
FT /evidence="ECO:0000250"
FT BINDING 420..425
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 862 AA; 95321 MW; BE09E32B28DD08B0 CRC64;
MKVTTVKELD EKLKVIKEAQ KKFSCYSQEM VDEIFRNAAM AAIDARIELA KAAVLETGMG
LVEDKVIKNH FAGEYIYNKY KDEKTCGIIE RNEPYGITKI AEPIGVVAAI IPVTNPTSTT
IFKSLISLKT RNGIFFSPHP RAKKSTILAA KTILDAAVKS GAPENIIGWI DEPSIELTQY
LMQKADITLA TGGPSLVKSA YSSGKPAIGV GPGNTPVIID ESAHIKMAVS SIILSKTYDN
GVICASEQSV IVLKSIYNKV KDEFQERGAY IIKKNELDKV REVIFKDGSV NPKIVGQSAY
TIAAMAGIKV PKTTRILIGE VTSLGEEEPF AHEKLSPVLA MYEADNFDDA LKKAVTLINL
GGLGHTSGIY ADEIKARDKI DRFSSAMKTV RTFVNIPTSQ GASGDLYNFR IPPSFTLGCG
FWGGNSVSEN VGPKHLLNIK TVAERRENML WFRVPHKVYF KFGCLQFALK DLKDLKKKRA
FIVTDSDPYN LNYVDSIIKI LEHLDIDFKV FNKVGREADL KTIKKATEEM SSFMPDTIIA
LGGTPEMSSA KLMWVLYEHP EVKFEDLAIK FMDIRKRIYT FPKLGKKAML VAITTSAGSG
SEVTPFALVT DNNTGNKYML ADYEMTPNMA IVDAELMMKM PKGLTAYSGI DALVNSIEAY
TSVYASEYTN GLALEAIRLI FKYLPEAYKN GRTNEKAREK MAHASTMAGM ASANAFLGLC
HSMAIKLSSE HNIPSGIANA LLIEEVIKFN AVDNPVKQAP CPQYKYPNTI FRYARIADYI
KLGGNTDEEK VDLLINKIHE LKKALNIPTS IKDAGVLEEN FYSSLDRISE LALDDQCTGA
NPRFPLTSEI KEMYINCFKK QP
