ID   ALDH_RHORT              Reviewed;         506 AA.
AC   Q9ZA11; Q2RVW3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Aldehyde dehydrogenase;
DE            EC=1.2.1.3;
GN   OrderedLocusNames=Rru_A0931;
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Okibe N., Amada K., Morikawa M., Kanaya S.;
RT   "Cloning of aldehyde dehydrogenase gene from photosynthetic bacterium
RT   Rhodospirillum rubrum.";
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
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   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AB006976; BAA75070.1; -; Genomic_DNA.
DR   EMBL; CP000230; ABC21732.1; -; Genomic_DNA.
DR   RefSeq; WP_011388686.1; NC_007643.1.
DR   RefSeq; YP_426019.1; NC_007643.1.
DR   AlphaFoldDB; Q9ZA11; -.
DR   SMR; Q9ZA11; -.
DR   STRING; 269796.Rru_A0931; -.
DR   EnsemblBacteria; ABC21732; ABC21732; Rru_A0931.
DR   KEGG; rru:Rru_A0931; -.
DR   PATRIC; fig|269796.9.peg.987; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_2_5; -.
DR   PhylomeDB; Q9ZA11; -.
DR   Proteomes; UP000001929; Chromosome.
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   CDD; cd07116; ALDH_ACDHII-AcoD; 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   PANTHER; PTHR43111; ALDEHYDE DEHYDROGENASE B-RELATED; 1.
DR   PANTHER; PTHR43111:SF1; ALDEHYDE DEHYDROGENASE B-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..506
FT                   /note="Aldehyde dehydrogenase"
FT                   /id="PRO_0000056454"
FT   ACT_SITE        262
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        301
FT                   /evidence="ECO:0000250"
FT   BINDING         218..224
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        165
FT                   /note="N -> K (in Ref. 1; BAA75070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        245
FT                   /note="G -> A (in Ref. 1; BAA75070)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   506 AA;  55419 MW;  8EBD79F820B149FD CRC64;
     MLYAAPGTAD AIFAFKPRYD NFIDGTWQPP VRGEYFDNVT PITGKVFCKA ARSTEEDITL
     ALDAAHAAAD RWGRTTAAER ALILNRIADR LQDNLETLAY VESIDNGKPI RETLAADIPL
     AIDHFRYFAA CIRAQEGSLS QIDETTIAYH FNEPLGVVGQ IIPWNFPILM ATWKLAPALA
     AGNCIVLKPA EQTPISILVL TELIADLLPP GVLNVVNGFG LEAGKPLASS KRIAKIAFTG
     ETATGRLIMQ YASQNLIPVT LELGGKSPNV FFDDIASADD SFFDKAVEGF VMFALNQGEI
     CTCPSRALIH ESLYDRFIER ALARVAVIKQ GSPLDTETMI GAQASTEQMD KILSYMDIGR
     EEGATVLAGG ARAELGGELD GGYYVQPTVF KGNNSMRIFQ EEIFGPVVAV TTFKDEDEAL
     HLANDTHYGL GSGVWTRDGN RAFRFGRGIK AGRVWTNCYH LYPAHAAFGG YKQSGIGREN
     HHMMLDHYQQ TKNLLVSYDP KAMGFF
//