ID Q0RJW5_FRAAA Unreviewed; 499 AA.
AC Q0RJW5;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:CAJ62195.1};
DE EC=1.2.1.3 {ECO:0000313|EMBL:CAJ62195.1};
GN OrderedLocusNames=FRAAL3552 {ECO:0000313|EMBL:CAJ62195.1};
OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ62195.1, ECO:0000313|Proteomes:UP000000657};
RN [1] {ECO:0000313|EMBL:CAJ62195.1, 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; CAJ62195.1; -; Genomic_DNA.
DR RefSeq; WP_011604693.1; NC_008278.1.
DR AlphaFoldDB; Q0RJW5; -.
DR STRING; 326424.FRAAL3552; -.
DR KEGG; fal:FRAAL3552; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_11; -.
DR OrthoDB; 6882680at2; -.
DR Proteomes; UP000000657; 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; cd07089; ALDH_CddD-AldA-like; 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 30..494
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 269
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 499 AA; 52353 MW; 28D037E5EC7B44E7 CRC64;
MTSATPTTPT APAVVGEARM LIDGRLVEAT GGAVYDNVNP ATEQVLGQTS DAAAVDLDAA
IAAARRAFDE SAWSTDRDLR RRCLTQLQQA LEGEREQLRA ELVAEAGAPV AVTGIAQLDW
PLADGLRGPL ELMDSFPWER SLPDTHLMGP SHRAVWQEPV GVVAAIVPWN FPFEVTINKL
GPAMATGNTV VLKPAPDTPW NATRIGRLIA EQTDIPPGVV NVVPCSDNAV AGQLLVDPRV
DMVSFTGSTG VGRLVVEKSA ATMKRTLLEL GGKSAMIILD DADLAAVLPL AGFGACLHSG
QGCALLTRVL LPRERYAEGV EILAGVIGAL PYGDPTDPAN LAGPLINARQ RERVLGYIEA
GRAQGARVVV GGGRPEHLPH GYYVQPTLLA DVDNTMTVAR EEIFGPVVCA IPFDGEADAV
RIANDSPYGL SGGVYSASVE RGLGVARRIR TGSINVNGGM FYGSDGPYGG FKQSGLGRQG
GLEGFASYTE AKTVGYVSA
//