ID   Q2K2Y7_RHIEC            Unreviewed;       512 AA.
AC   Q2K2Y7;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=aldehyde dehydrogenase (NAD(+)) {ECO:0000256|ARBA:ARBA00024226};
DE            EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
GN   OrderedLocusNames=RHE_CH04055 {ECO:0000313|EMBL:ABC92799.1};
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC92799.1, ECO:0000313|Proteomes:UP000001936};
RN   [1] {ECO:0000313|EMBL:ABC92799.1, ECO:0000313|Proteomes:UP000001936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP000133; ABC92799.1; -; Genomic_DNA.
DR   RefSeq; WP_011427241.1; NC_007761.1.
DR   AlphaFoldDB; Q2K2Y7; -.
DR   KEGG; ret:RHE_CH04055; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_2_5; -.
DR   OrthoDB; 9812625at2; -.
DR   Proteomes; UP000001936; 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; cd07130; ALDH_F7_AASADH; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR044638; ALDH7A1-like.
DR   PANTHER; PTHR43521; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43521:SF1; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001936}.
FT   DOMAIN          29..490
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   512 AA;  54166 MW;  6DCC1133EC78C3D1 CRC64;
     MTIAVLDLAT ETAKLLAELG VDAGRYHGGT LSVTSPVTGK EIGKLREHTV SETKAAIEEA
     HKAFLEWRDV PAPKRGELVR LLGEELRAAK TALGRLVSIE VGKITSEGLG EVQEMIDICD
     FAVGLSRQLY GLTIATERSE HRMMESWHPL GAIGIISAFN FPVAVWSWNA ALAMVCGNST
     VWKPSEKTPL TALAVQALFE KALKRFVAEG GKAPANLSTL IIGGREVGEV LVDHPKIPLV
     SATGSTAMGR AVGPRLSQRF ARAILELGGN NAAIVCPSAD LDLTLRGVAF SAMGTAGQRC
     TTLRRLFVHD SVYDQLVPRL QKAYGSVTIG NPLEAGTLVG PLIDGQAFEK MQAALGEAKS
     AGGKVTGGER VDNGSADAFY VRPALVEMPA QTGPVEHETF APILYVMKYS DFDAVLALHN
     AVPQGLSSSI FTNDMREAET FVSARGSDCG IANVNLGPSG AEIGGAFGGE KETGGGRESG
     SDAWKAYMRR ATNTINYGST LPLAQGVKFD VE
//