ID   AL7A1_PEA               Reviewed;         508 AA.
AC   P25795;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Aldehyde dehydrogenase family 7 member A1;
DE            EC=1.2.1.3;
DE   AltName: Full=Antiquitin-1;
DE   AltName: Full=Turgor-responsive protein 26G;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Progress No. 9;
RX   PubMed=1715781; DOI=10.1007/bf00017720;
RA   Guerrero F.D., Jones J.T., Mullet J.E.;
RT   "Turgor-responsive gene transcription and RNA levels increase rapidly when
RT   pea shoots are wilted. Sequence and expression of three inducible genes.";
RL   Plant Mol. Biol. 15:11-26(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-16.
RX   PubMed=11959129; DOI=10.1016/s0014-5793(02)02553-x;
RA   Tang W.-K., Cheng C.H.K., Fong W.-P.;
RT   "First purification of the antiquitin protein and demonstration of its
RT   enzymatic activity.";
RL   FEBS Lett. 516:183-186(2002).
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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- INDUCTION: By dehydration of shoots but not roots and not by heat shock
CC       or ABA.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X54359; CAA38243.1; -; mRNA.
DR   PIR; S11863; S11863.
DR   AlphaFoldDB; P25795; -.
DR   SMR; P25795; -.
DR   PRIDE; P25795; -.
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   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 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; PTHR43521; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11959129"
FT   CHAIN           2..508
FT                   /note="Aldehyde dehydrogenase family 7 member A1"
FT                   /id="PRO_0000056498"
FT   ACT_SITE        266
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        300
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   BINDING         244..249
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            165
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   508 AA;  53789 MW;  CC88F367B52E923D CRC64;
     MGSDSNNLGF LKEIGLGATN IGSFINGQWK ANGPTVHSVN PSTNQVIASV TEATLDDYEE
     GLRASSEAAK TWRTVPAPKR GEIVRQIGDA LRAKLDPLGR LVALEMGKIL AEGIGEVQEI
     IDMCDYSVGL SRQLNGSIIP SERPEHMMFE VWNPLGIVGV ITAFNFPCAV LGWNACIALV
     GGNTVVWKGA PTTPLITVAV TKLIAEVFER NNLPGAIFTA LCGGADIGHA IAKDTRIPLV
     SFTGSSKVGA LVQQTVSQRF GKTLLELSGN NAIIVMDDAD ITLAVRSIFF AAVGTAGQRC
     TTCRRLYLHE SVYANVLEQL TALYKQVKIG NPLEEGTLVG PLHTRSAVEN FKNGISAIKS
     QGGKIVTGGS VLESEGNFVV PTIVEISADA AVVKEELFAP VLYVMKFKDL EEAIALNNSV
     PQGLSSSIFT QKPSTIFKWI GPSGSDCGIV NVNIPTNGAE IGGAFGGEKA TGGGREAGSD
     SWKQYMRRST CTINYGSELP LAQGINFG