ID   ALDH_LINUS              Reviewed;         551 AA.
AC   Q40255;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   22-FEB-2023, entry version 81.
DE   RecName: Full=Probable aldehyde dehydrogenase;
DE            EC=1.2.1.3;
DE   AltName: Full=Flax-inducible sequence 1;
GN   Name=FIS1;
OS   Linum usitatissimum (Flax) (Linum humile).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Linaceae; Linum.
OX   NCBI_TaxID=4006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   STRAIN=cv. Hoshangabad; TISSUE=Seedling leaf;
RX   PubMed=7655501; DOI=10.1046/j.1365-313x.1995.08010001.x;
RA   Roberts J.K., Pryor A.;
RT   "Isolation of a flax (Linum usitatissimum) gene induced during susceptible
RT   infection by flax rust (Melampsora lini).";
RL   Plant J. 8:1-8(1995).
CC   -!- FUNCTION: Could be involved in facilitating the biotrophic relationship
CC       between the plant and the rust fungus.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.3;
CC   -!- TISSUE SPECIFICITY: In uninfected plants, highest levels found in
CC       stems. In plants infected with the flax rust, highest levels in leaves.
CC       Higher levels of expression in infected leaves than uninfected stems.
CC   -!- INDUCTION: By flax rust susceptible infection but not by resistant
CC       infection. Levels 10-fold higher in infected plants than uninfected
CC       plants. {ECO:0000269|PubMed:7655501}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; X86733; CAA60412.1; -; mRNA.
DR   AlphaFoldDB; Q40255; -.
DR   SMR; Q40255; -.
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; cd07126; ALDH_F12_P5CDH; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
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:SF7; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 12A1, MITOCHONDRIAL; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   2: Evidence at transcript level;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..551
FT                   /note="Probable aldehyde dehydrogenase"
FT                   /id="PRO_0000056433"
FT   ACT_SITE        297
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        332
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         278..283
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            203
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   551 AA;  61032 MW;  F1B87A79D76E863E CRC64;
     MYRPLVARLL RDSVATRKGS SHFARRFSHS LPFATVDAEE LSGAKPAEVL NLVQGNWGGS
     SSWHTVVDPL NGEPFIKVAE VDETEIKPFV ESLSKCPKHG LHNPFKSPER YLLYGDISTK
     AGHMLSIPKV SEFFARLIQR VAPKSYHQAL GEVQVTQKFF ENFTGDQVRF LARSFGVPGN
     HLGQQSNGFR WPFGPVAIIT PFNFPLEIPV LQLMGALYMG NKPLLKVDSK VSIVMEQMMR
     LLHYCGLPVG DADFVNSDGK AMNKILLEAN PRMTLFTGSS RVAEKLALDL KGRIKLEDAG
     FDWKILGPDV NEADYVAWVC DQDAYACSGQ KCSAQSILFM HENWAATPLI SRLKELAERR
     KLEDLTVGPV LTVTTEAMLD HLNKLLQIPG AKLLFGGKPL ENHTIPSIYG AVKPTAVYVP
     LEEILKVSNY ELVTKEIFGP FQVVTEYKNS QLPMVLEALE RMHAHLTAAV VSNDQLFLQE
     VIGNTVNGTT YAGLRARTTG APQNHWFGPA GDPRGAGIGT PEAIKLVWSC HREIIYDIGP
     VSHHWEIPPS T
//