ID   AL7A1_MALDO             Reviewed;         508 AA.
AC   Q9ZPB7;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Aldehyde dehydrogenase family 7 member A1;
DE            EC=1.2.1.3;
DE   AltName: Full=Antiquitin-1;
DE   AltName: Full=Matured fruit 60 kDa protein;
DE            Short=MF-60;
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000312|EMBL:BAA75633.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-31 AND 386-404, AND
RP   INDUCTION.
RC   STRAIN=cv. Fuji; TISSUE=Fruit;
RX   PubMed=10202815; DOI=10.1093/oxfordjournals.pcp.a029528;
RA   Yamada K., Mori H., Yamaki S.;
RT   "Identification and cDNA cloning of a protein abundantly expressed during
RT   apple fruit development.";
RL   Plant Cell Physiol. 40:198-204(1999).
CC   -!- FUNCTION: May play a role in fruit development.
CC       {ECO:0000303|PubMed:10202815}.
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|UniProtKB:P83402}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in developing fruit during the
CC       enlargement stage. {ECO:0000269|PubMed:10202815}.
CC   -!- INDUCTION: By osmotic pressure changes. {ECO:0000303|PubMed:10202815,
CC       ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; D88434; BAA75633.1; -; mRNA.
DR   RefSeq; NP_001281025.1; NM_001294096.1.
DR   AlphaFoldDB; Q9ZPB7; -.
DR   SMR; Q9ZPB7; -.
DR   STRING; 3750.XP_008337836.1; -.
DR   PRIDE; Q9ZPB7; -.
DR   GeneID; 103400922; -.
DR   KEGG; mdm:103400922; -.
DR   OrthoDB; 692580at2759; -.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; ISS:UniProtKB.
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.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10202815"
FT   CHAIN           2..508
FT                   /note="Aldehyde dehydrogenase family 7 member A1"
FT                   /id="PRO_0000056497"
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;  54244 MW;  FCE5487F10DEDABA CRC64;
     MGFAKKEHEF LSAIGLAPEN PGGFINGKWK ASGPVISTVS PSNNQEIAKV TEVSMEEYEE
     GLRSCNDAAK TWKSLPAPKR GEIVRQIGDA LREKLQHLGK LVSLEMGKIL AEGIGEVQEV
     IYMCDFAVGL SRQLNGSIIP SERPDHMMFE VWNPLGIVGV ITAFNFPCAV LGWNACIALV
     CGNCVVWKGA PTTPLVTIAV TKLIAEVLEK NNLPAAIFTA FCGGAEIGEA IAKDTRIPLV
     SFTGSSKVGA KVQQIVTERF GKCLLELSGN NALIVMDDAD VGLAVRSIFF AAVGTAGQRC
     TTCRRLYLHE SIYQNVLDKL VGLYNQVKIG DPLEEGTLVG PVHTKASREN FEKGISTIKS
     QGGKILTGGS VIESDGNFVQ PTIVEIASNA SVVKEELFGP VLYVMKFKTL EEAIALNNSV
     PQGLSSSIFT SKPNTIFKWI GPHGSDCGIV NVNIPTNGAE IGGAFGGEKA TGGGREAGSD
     SWKQYMRRST CTINYGTELP LAQGINFG