ALDB_ECOLI
ID ALDB_ECOLI Reviewed; 512 AA.
AC P37685; P78118; Q2M7Q1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Aldehyde dehydrogenase B {ECO:0000303|PubMed:15659684};
DE EC=1.2.1.4 {ECO:0000269|PubMed:15659684};
DE AltName: Full=Acetaldehyde dehydrogenase {ECO:0000303|PubMed:15659684};
GN Name=aldB {ECO:0000303|PubMed:15659684}; Synonyms=yiaX;
GN OrderedLocusNames=b3588, JW3561;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TRANSCRIPTION REGULATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7768815; DOI=10.1128/jb.177.11.3166-3175.1995;
RA Xu J., Johnson R.C.;
RT "aldB, an RpoS-dependent gene in Escherichia coli encoding an aldehyde
RT dehydrogenase that is repressed by Fis and activated by Crp.";
RL J. Bacteriol. 177:3166-3175(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MASS
RP SPECTROMETRY, MUTAGENESIS OF ARG-197, AND SUBUNIT.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=15659684; DOI=10.1128/jb.187.3.1067-1073.2005;
RA Ho K.K., Weiner H.;
RT "Isolation and characterization of an aldehyde dehydrogenase encoded by the
RT aldB gene of Escherichia coli.";
RL J. Bacteriol. 187:1067-1073(2005).
CC -!- FUNCTION: Catalyzes the NADP(+)-dependent oxidation of diverse
CC aldehydes to their corresponding carboxylic acids, with a preference
CC for acetaldehyde and chloroacetaldehyde (PubMed:15659684). May play a
CC role in detoxifying aldehydes present during stationary phase
CC (Probable). Cannot use NAD(+) instead of NADP(+) as the electron
CC acceptor. To a lesser extent is also able to oxidize propionaldehyde
CC (propanal), benzaldehyde, mafosfamide, and 4-
CC hydroperoxycyclophosphamide. Does not use either glyceraldehyde or
CC glycolaldehyde as substrates (PubMed:15659684).
CC {ECO:0000269|PubMed:15659684, ECO:0000305|PubMed:7768815}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NADP(+) = a carboxylate + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:11888, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.4;
CC Evidence={ECO:0000269|PubMed:15659684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetaldehyde + H2O + NADP(+) = acetate + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:25298, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.4;
CC Evidence={ECO:0000269|PubMed:15659684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloroacetaldehyde + H2O + NADP(+) = chloroacetate + 2 H(+) +
CC NADPH; Xref=Rhea:RHEA:62248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:23123, ChEBI:CHEBI:27871, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:15659684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) + propanal = 2 H(+) + NADPH + propanoate;
CC Xref=Rhea:RHEA:27918, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17153, ChEBI:CHEBI:17272, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:15659684};
CC -!- ACTIVITY REGULATION: Magnesium increases enzyme activity with various
CC substrates. {ECO:0000269|PubMed:15659684}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.5 uM for acetaldehyde {ECO:0000269|PubMed:15659684};
CC KM=3.6 uM for chloroacetaldehyde {ECO:0000269|PubMed:15659684};
CC KM=5.8 uM for propionaldehyde {ECO:0000269|PubMed:15659684};
CC KM=56.8 uM for benzaldehyde {ECO:0000269|PubMed:15659684};
CC KM=900 uM for 4-hydroperoxycyclophosphamide
CC {ECO:0000269|PubMed:15659684};
CC KM=65 uM for NADP {ECO:0000269|PubMed:15659684};
CC Vmax=2 umol/min/mg enzyme with acetaldehyde as substrate
CC {ECO:0000269|PubMed:15659684};
CC Vmax=3.3 umol/min/mg enzyme with chloroacetaldehyde as substrate
CC {ECO:0000269|PubMed:15659684};
CC Vmax=1 umol/min/mg enzyme with propionaldehyde as substrate
CC {ECO:0000269|PubMed:15659684};
CC Vmax=0.6 umol/min/mg enzyme with benzaldehyde as substrate
CC {ECO:0000269|PubMed:15659684};
CC Vmax=0.2 umol/min/mg enzyme with 4-hydroperoxycyclophosphamide
CC {ECO:0000269|PubMed:15659684};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15659684}.
CC -!- INDUCTION: Is repressed by Fis. Positively regulated by RpoS and Crp.
CC Induced by ethanol. Expression is maximally induced during the
CC transition from exponential phase to stationary phase.
CC {ECO:0000269|PubMed:7768815}.
CC -!- MASS SPECTROMETRY: Mass=56352; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15659684};
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18565.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L40742; AAC36939.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18565.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76612.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77705.1; -; Genomic_DNA.
DR PIR; S47809; S47809.
DR RefSeq; NP_418045.4; NC_000913.3.
DR RefSeq; WP_000183980.1; NZ_SSZK01000041.1.
DR AlphaFoldDB; P37685; -.
DR SMR; P37685; -.
DR BioGRID; 4262555; 18.
DR DIP; DIP-9082N; -.
DR IntAct; P37685; 3.
DR MINT; P37685; -.
DR STRING; 511145.b3588; -.
DR jPOST; P37685; -.
DR PaxDb; P37685; -.
DR PRIDE; P37685; -.
DR EnsemblBacteria; AAC76612; AAC76612; b3588.
DR EnsemblBacteria; BAE77705; BAE77705; BAE77705.
DR GeneID; 948104; -.
DR KEGG; ecj:JW3561; -.
DR KEGG; eco:b3588; -.
DR PATRIC; fig|1411691.4.peg.3123; -.
DR EchoBASE; EB2200; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_2_6; -.
DR InParanoid; P37685; -.
DR OMA; HGIGYYP; -.
DR PhylomeDB; P37685; -.
DR BioCyc; EcoCyc:ALDDEHYDROGB-MON; -.
DR BioCyc; MetaCyc:ALDDEHYDROGB-MON; -.
DR SABIO-RK; P37685; -.
DR PRO; PR:P37685; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:EcoliWiki.
DR GO; GO:0033721; F:aldehyde dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:EcoliWiki.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0045471; P:response to ethanol; IDA:EcoliWiki.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Magnesium; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..512
FT /note="Aldehyde dehydrogenase B"
FT /id="PRO_0000056565"
FT ACT_SITE 268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT MUTAGEN 197
FT /note="R->E: Less than 10% of wild-type acetaldehyde
FT dehydrogenase activity."
FT /evidence="ECO:0000269|PubMed:15659684"
SQ SEQUENCE 512 AA; 56306 MW; E673C34340DF68CD CRC64;
MTNNPPSAQI KPGEYGFPLK LKARYDNFIG GEWVAPADGE YYQNLTPVTG QLLCEVASSG
KRDIDLALDA AHKVKDKWAH TSVQDRAAIL FKIADRMEQN LELLATAETW DNGKPIRETS
AADVPLAIDH FRYFASCIRA QEGGISEVDS ETVAYHFHEP LGVVGQIIPW NFPLLMASWK
MAPALAAGNC VVLKPARLTP LSVLLLMEIV GDLLPPGVVN VVNGAGGVIG EYLATSKRIA
KVAFTGSTEV GQQIMQYATQ NIIPVTLELG GKSPNIFFAD VMDEEDAFFD KALEGFALFA
FNQGEVCTCP SRALVQESIY ERFMERAIRR VESIRSGNPL DSVTQMGAQV SHGQLETILN
YIDIGKKEGA DVLTGGRRKL LEGELKDGYY LEPTILFGQN NMRVFQEEIF GPVLAVTTFK
TMEEALELAN DTQYGLGAGV WSRNGNLAYK MGRGIQAGRV WTNCYHAYPA HAAFGGYKQS
GIGRETHKMM LEHYQQTKCL LVSYSDKPLG LF
