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Database: UniProt
Entry: Q0RF45_FRAAA
LinkDB: Q0RF45_FRAAA
Original site: Q0RF45_FRAAA 
ID   Q0RF45_FRAAA            Unreviewed;       502 AA.
AC   Q0RF45;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Putative aldehyde dehydrogenase {ECO:0000313|EMBL:CAJ63906.1};
DE            EC=1.2.1.- {ECO:0000313|EMBL:CAJ63906.1};
GN   OrderedLocusNames=FRAAL5273 {ECO:0000313|EMBL:CAJ63906.1};
OS   Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ63906.1, ECO:0000313|Proteomes:UP000000657};
RN   [1] {ECO:0000313|EMBL:CAJ63906.1, ECO:0000313|Proteomes:UP000000657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CT573213; CAJ63906.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0RF45; -.
DR   STRING; 326424.FRAAL5273; -.
DR   KEGG; fal:FRAAL5273; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_0_11; -.
DR   Proteomes; UP000000657; Chromosome.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd07139; ALDH_AldA-Rv0768; 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   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; 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:UP000000657}.
FT   DOMAIN          33..496
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        270
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   502 AA;  52037 MW;  2249499009644D88 CRC64;
     MPADEDPRIR RGIRDDRGVG VREHRELFID GRWVGATTEE TLAVVSPATE ETIGVVAAAG
     IGDVDRAVAA ARRALDDGPW ARATPPQRVA ALVRLADALR ARADELAEVL TAEVGSPRSW
     SQPYQVGTAL AAFDAFAALA GDYPWADERP AAHGSVLVRR LPVGVVGAVV PWNAPLFITA
     LKLGPALVAG CTVVLKPAPA APVWSYLFAE AVVEAGLPPG VVNIVPAGTA ASEYLVGHPG
     VDKVTFTGST AVGRRIGEVC GRDLRRCTLE LGGKSAAILL DDVSLTRRTV TTLTFGAMAN
     SGQVCMAQTR ILAPRSRYSE VVDALAERVA ALRVGDPTEP KTQIGPVISA SARARIEAHL
     ARARTDGARV AAGGGRPAGL DRGWFVEPTL LAGVGNDAPV AREEIFGPVA VVIPYDGVEE
     AVTLANDSDY GLAGSVWSED PERAGRVAAR LRTGSVAVNS PAPLDPGSPF GGMGASGIGR
     EGGPEGVDAF VELQSIIRPA DG
//
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