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 24-JAN-2024, entry version 101.
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) (Lathyrus oleraceus).
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}.
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DR EMBL; X54359; CAA38243.1; -; mRNA.
DR PIR; S11863; S11863.
DR AlphaFoldDB; P25795; -.
DR SMR; 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 CDD; cd07130; ALDH_F7_AASADH; 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; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43521:SF1; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 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
//
