ID   G9A3I4_RHIFH            Unreviewed;       510 AA.
AC   G9A3I4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=aldehyde dehydrogenase (NAD(+)) {ECO:0000256|ARBA:ARBA00024226};
DE            EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
GN   OrderedLocusNames=SFHH103_03441 {ECO:0000313|EMBL:CCE97932.1};
OS   Rhizobium fredii (strain HH103) (Sinorhizobium fredii).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=1117943 {ECO:0000313|EMBL:CCE97932.1, ECO:0000313|Proteomes:UP000007735};
RN   [1] {ECO:0000313|EMBL:CCE97932.1, ECO:0000313|Proteomes:UP000007735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HH103 {ECO:0000313|EMBL:CCE97932.1,
RC   ECO:0000313|Proteomes:UP000007735};
RX   PubMed=22374952; DOI=10.1128/JB.06729-11;
RA   Weidner S., Becker A., Bonilla I., Jaenicke S., Lloret J., Margaret I.,
RA   Puhler A., Ruiz-Sainz J.E., Schneiker-Bekel S., Szczepanowski R.,
RA   Vinardell J.M., Zehner S., Gottfert M.;
RT   "Genome sequence of the soybean symbiont Sinorhizobium fredii HH103.";
RL   J. Bacteriol. 194:1617-1618(2012).
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; HE616890; CCE97932.1; -; Genomic_DNA.
DR   RefSeq; WP_014330315.1; NC_016812.1.
DR   AlphaFoldDB; G9A3I4; -.
DR   STRING; 1117943.SFHH103_03441; -.
DR   GeneID; 48974922; -.
DR   KEGG; sfh:SFHH103_03441; -.
DR   PATRIC; fig|380.5.peg.3637; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_2_5; -.
DR   Proteomes; UP000007735; 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}.
FT   DOMAIN          32..488
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   510 AA;  54187 MW;  12DA1A2CA2018333 CRC64;
     MNIAAKKIDV AKEAAALLDK LGVAKELYTG GDMPSFSPVT GEQIASLRTV SAAEAAKQIE
     KADEAFRAWR LVPAPKRGEL VRLLGEELRA FKADLGRLVS LEAGKIPSEG LGEVQEMIDI
     CDFAVGLSRQ LYGLTIATER PGHRMMETWH PLGVVGIISA FNFPVAVWSW NAALALVCGN
     AVVWKPSEKT PLTALACEAI LERALARFGD APEGLSQVLI GDRSIGEVLV DHPKVPLVSA
     TGSTRMGREV GPRLAKRFAR SILELGGNNA GIVCPSADLD MALRAIAFGA MGTAGQRCTT
     LRRLFVHESV YDQLVPRLKK AYASVSVGNP LESTALVGPL VDKAAFDNMQ KAISEAKAEG
     GAVTGGERVE LGYDNGYYVK PALVEMPKQA GPVLEETFAP ILYVIKYSDF DAVLAEHNAV
     AAGLSSSIFT RDMQESERFL AADGSDCGIA NVNIGTSGAE IGGAFGGEKE TGGGRESGSD
     AWRAYMRRAT NTINYSKALP LAQGVSFDIE
//