ID Q99Q18_STRCO Unreviewed; 293 AA.
AC Q99Q18;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Acetaldehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01657};
DE EC=1.2.1.10 {ECO:0000256|HAMAP-Rule:MF_01657};
DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] {ECO:0000256|HAMAP-Rule:MF_01657};
GN OrderedLocusNames=SCP1.300 {ECO:0000313|EMBL:CAC36825.1}, SCP1.54c
GN {ECO:0000313|EMBL:CAC36576.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OG Plasmid SCP1 {ECO:0000313|Proteomes:UP000001973}.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAC36825.1, ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAC36825.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A3 {ECO:0000313|EMBL:CAC36825.1};
RC PLASMID=SCP1 {ECO:0000313|Proteomes:UP000001973};
RX PubMed=9573173;
RA Redenbach M., Ikeda K., Yamasaki M., Kinashi H.;
RT "Cloning and physical mapping of the EcoRI fragments of the giant linear
RT plasmid SCP1.";
RL J. Bacteriol. 180:2796-2799(1998).
RN [2] {ECO:0000313|EMBL:CAC36825.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A3 {ECO:0000313|EMBL:CAC36825.1};
RC PLASMID=SCP1 {ECO:0000313|Proteomes:UP000001973};
RA Bentley S.D., Parkhill J., Barrell B.G., Rajandream M.A.;
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145
RC {ECO:0000313|Proteomes:UP000001973};
RC PLASMID=SCP1 {ECO:0000313|Proteomes:UP000001973};
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [4] {ECO:0000313|EMBL:CAC36825.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A3 {ECO:0000313|EMBL:CAC36825.1};
RC PLASMID=SCP1 {ECO:0000313|Proteomes:UP000001973};
RX PubMed=18988741; DOI=10.1073/pnas.0805530105;
RA Corre C., Song L., O'Rourke S., Chater K.F., Challis G.L.;
RT "2-Alkyl-4-hydroxymethylfuran-3-carboxylic acids, antibiotic production
RT inducers discovered by Streptomyces coelicolor genome mining.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:17510-17515(2008).
RN [5] {ECO:0000313|EMBL:CAC36825.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A3 {ECO:0000313|EMBL:CAC36825.1};
RC PLASMID=SCP1 {ECO:0000313|Proteomes:UP000001973};
RX PubMed=19054329; DOI=10.1111/j.1365-2958.2008.06560.x;
RA O'Rourke S., Wietzorrek A., Fowler K., Corre C., Challis G.L., Chater K.F.;
RT "Extracellular signalling, translational control, two repressors and an
RT activator all contribute to the regulation of methylenomycin production in
RT Streptomyces coelicolor.";
RL Mol. Microbiol. 71:763-778(2009).
RN [6] {ECO:0000313|EMBL:CAC36825.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A3 {ECO:0000313|EMBL:CAC36825.1};
RC PLASMID=SCP1 {ECO:0000313|Proteomes:UP000001973};
RA Brown S.P., Murphy L.D., Harris D.;
RT ".";
RL Submitted (FEB-2015) 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:0000256|HAMAP-
CC Rule:MF_01657};
CC -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009244, ECO:0000256|HAMAP-Rule:MF_01657}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01657}.
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DR EMBL; AL589148; CAC36576.1; -; Genomic_DNA.
DR EMBL; AL589148; CAC36825.1; -; Genomic_DNA.
DR RefSeq; NP_639629.1; NC_003903.1.
DR RefSeq; NP_639909.1; NC_003903.1.
DR AlphaFoldDB; Q99Q18; -.
DR STRING; 100226.gene:17765560; -.
DR PATRIC; fig|100226.15.peg.8002; -.
DR HOGENOM; CLU_062208_0_0_11; -.
DR OrthoDB; 9786743at2; -.
DR Proteomes; UP000001973; Plasmid SCP1.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism {ECO:0000256|HAMAP-Rule:MF_01657};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01657};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01657};
KW Reference proteome {ECO:0000313|Proteomes:UP000001973}.
FT DOMAIN 8..121
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 129
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
SQ SEQUENCE 293 AA; 30594 MW; D5908995517643D7 CRC64;
MTPHARLNTA VLGTGPLGLD LIERIHASPY LNSPLVVGHR PGSRGLAQAA DLGCVTRSGG
IDAVLDADRS VDVVFDATNA FAHPAHWDKL ADTGAILIDL TPTTTGTLIV PTVNGHQAAH
HQHIGLVSCS GQAALPILHA VTSRHPAAAV EMVATAASAS VGRASRLNLD EYLDTTQQAI
RCFTHAPDAK TMINISAATP APPFRTAITV ITADPAPADD IATLTASVEQ KMRALVPGYH
VTSCTSEDRT VRVVVEVTAT RSRIPVHAGN LEVISAAAIH AAEQRAQHQE AHS
//
