ID Q0RTV7_FRAAA Unreviewed; 494 AA.
AC Q0RTV7;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:CAJ58991.1};
DE EC=1.2.1.3 {ECO:0000313|EMBL:CAJ58991.1};
GN OrderedLocusNames=FRAAL0315 {ECO:0000313|EMBL:CAJ58991.1};
OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ58991.1, ECO:0000313|Proteomes:UP000000657};
RN [1] {ECO:0000313|EMBL:CAJ58991.1, 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; CAJ58991.1; -; Genomic_DNA.
DR RefSeq; WP_011601571.1; NC_008278.1.
DR AlphaFoldDB; Q0RTV7; -.
DR STRING; 326424.FRAAL0315; -.
DR KEGG; fal:FRAAL0315; -.
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 28..490
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 265
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 494 AA; 52501 MW; 7DC8D5C2491A286B CRC64;
MTTASEAVSL QGEPRLLIDG KLGESATGSR YDNINPATEE ILGQTTDATA ADMDRAIAAA
RRAFDESSWS TDRELRKRCL AQLQAALDDE KEALRAELIA EAGAPIAVTH FAQLDWPLAD
GLRGPLELID TFPWERTLPD TNLFGPSHRA VWKEPVGVVA AIVPWNYPFE VTINKLGPIL
ATGNTVVLKP APDTPWNATR IGRIVAERTD IPAGVVNVVP TSDNAVAELL VTDPRVDMVS
FTGSTGIGRR IVELSAGTMK RTLLELGGKS AMIVLDDADL ASVLPGAGLG ACLHAGQGCA
MTTRILLPRS VYDQGLEILT EVFRHLPYGD PNDPANLSGP QINARQRDRV LDYIEIGKAE
GARVVAGGGR PAHLPTGYYV EPTLLADVDN GMRVAREEIF GPVAAVIPFD DEADAVRIAN
DSPYGLSGGV FSASLDRGLS VARRIRTGSI NVNGGNFYGS NGPYGGYKLS GNGRQGGIEG
FEQHLESKSV GFAG
//
