ID   A9BR24_DELAS            Unreviewed;       485 AA.
AC   A9BR24;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=Aldehyde Dehydrogenase {ECO:0000313|EMBL:ABX32979.1};
GN   OrderedLocusNames=Daci_0333 {ECO:0000313|EMBL:ABX32979.1};
OS   Delftia acidovorans (strain DSM 14801 / SPH-1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX32979.1, ECO:0000313|Proteomes:UP000000784};
RN   [1] {ECO:0000313|EMBL:ABX32979.1, ECO:0000313|Proteomes:UP000000784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX   PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA   Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT   "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT   defined pairs of heterotrophic bacteria.";
RL   Appl. Environ. Microbiol. 70:4053-4063(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT   "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00024149};
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DR   EMBL; CP000884; ABX32979.1; -; Genomic_DNA.
DR   RefSeq; WP_012202272.1; NC_010002.1.
DR   AlphaFoldDB; A9BR24; -.
DR   STRING; 398578.Daci_0333; -.
DR   GeneID; 24115950; -.
DR   KEGG; dac:Daci_0333; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_2_4; -.
DR   Proteomes; UP000000784; Chromosome.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProt.
DR   GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
DR   CDD; cd07138; ALDH_CddD_SSP0762; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   PANTHER; PTHR42804; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42804:SF1; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000784}.
FT   DOMAIN          15..474
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   485 AA;  51240 MW;  C99B875F093F4FDD CRC64;
     MSTQEHLQFY IDGQWVPPAV PRTLDVINPS TEEVAARISM GSAADVDAAV AAARRAFDGF
     SQTTRDERLA LLDKVLAVYM RRIDEVAQTI SLEMGAPLWL SRAAQATVGA GHLKQTLQVL
     RDFEFESVRG TTGIVHEPVG VVGMITPWNW PINQIMCKVA PALAAGCTMV LKPSEIAPLN
     AILVAEILHE AGVPAGVFNL VNGDGPSVGE AMSVHPGIDM MTFTGSTRAG IAVAKASADT
     VKRVTQELGG KSANIVLDDA DIEKAVAQGV NACFTNSGQS CNAPTRMFVP RAMHARAVAA
     AKAAAEGVKV GDALADTGAM HMGPVVSEAQ FRKIQGLIEA GIAEGATLVA GGTGRPEGLA
     RGYFVRPTVF ADVRNDMTIA REEIFGPVLV ILPYDTEEEA IAQANDTPYG LSGYVQSGSL
     ERARRVASRL RTGMVHLNGA GPDFGAPFGG YKQSGTGREW GEHGFKEYLE VKAVMGYQPK
     QKAAA
//