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Database: UniProt/TrEMBL
Entry: B3QEP3_RHOPT
LinkDB: B3QEP3_RHOPT
Original site: B3QEP3_RHOPT 
ID   B3QEP3_RHOPT            Unreviewed;       476 AA.
AC   B3QEP3;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Aldehyde Dehydrogenase {ECO:0000313|EMBL:ACF00959.1};
GN   OrderedLocusNames=Rpal_2445 {ECO:0000313|EMBL:ACF00959.1};
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960 {ECO:0000313|EMBL:ACF00959.1, ECO:0000313|Proteomes:UP000001725};
RN   [1] {ECO:0000313|EMBL:ACF00959.1, ECO:0000313|Proteomes:UP000001725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1 {ECO:0000313|EMBL:ACF00959.1,
RC   ECO:0000313|Proteomes:UP000001725};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA   Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-2008) 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; CP001096; ACF00959.1; -; Genomic_DNA.
DR   RefSeq; WP_012495713.1; NC_011004.1.
DR   AlphaFoldDB; B3QEP3; -.
DR   KEGG; rpt:Rpal_2445; -.
DR   HOGENOM; CLU_005391_0_2_5; -.
DR   OrthoDB; 9812625at2; -.
DR   Proteomes; UP000001725; 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}.
FT   DOMAIN          13..470
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   476 AA;  50489 MW;  5150BF355718DCB6 CRC64;
     MVNRMQFYID GAWVDPVVKK STPVVNPATE EAMYEVALGS KADVDKAVAA AKRAFETFSV
     TSREERIALL EKVVAVYKSR MKEIGAAISD EMGAPLPMAE KMQAGAGLGH IMSTLDVLKN
     YQFEEPLGSA MIVREPIGVV GMITPWNWPL NQIACKVAPA IAAGCTMVLK PSEFTPTSAL
     LFAEILHEAG VPKGVFNLVN GLGPEVGAAM SEHPDIDMIS FTGSTRAGID VAQRAAPTVK
     RVSQELGGKS PNVILEDADL TKAVTGGVMH MFNNSGQSCN APSRMIVPLS KMKEVAAIAK
     GVAEKTKAGD PRGEGTTIGP VVNRIQWDKI QTLINKGIEE GATLVAGGPG LPEGVNKGFY
     VRPTVFADVT KDMTIAREEI FGPVLVIMGA KDENEAVELA NDTPYGLAGY VSAGSVDRAR
     AVGRKIRAGN VNLQGVPNER TAPFGGYKQS GNGREWGKFG LEEYLEVKAI AGFNAA
//
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