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 04-NOV-2008, entry version 53. DE RecName: Full=Aldehyde dehydrogenase family 7 member A1; DE EC=1.2.1.3; DE AltName: Full=Turgor-responsive protein 26G; DE AltName: Full=Antiquitin-1; OS Pisum sativum (Garden pea). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Fabeae; Pisum. OX NCBI_TaxID=3888; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Progress No. 9; RX MEDLINE=91355842; 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 RT when pea shoots are wilted. Sequence and expression of three inducible RT genes."; RL Plant Mol. Biol. 15:11-26(1990). RN [2] RP PROTEIN SEQUENCE OF 2-16. RX MEDLINE=21956475; 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: An aldehyde + NAD(+) + H(2)O = an acid + NADH. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- INDUCTION: By dehydration of shoots but not roots and not by heat CC shock or ABA. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X54359; CAA38243.1; -; mRNA. DR PIR; S11863; S11863. DR HSSP; P51977; 1BXS. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW. DR InterPro; IPR016160; Ald_DHase_CS. DR InterPro; IPR016162; Ald_DHase_N. DR InterPro; IPR015590; Aldehyde_DHase. DR Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1. DR PANTHER; PTHR11699; Aldehyde_dehyd; 1. DR Pfam; PF00171; Aldedh; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; FALSE_NEG. 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 1 Removed. FT CHAIN 2 508 Aldehyde dehydrogenase family 7 member FT A1. FT /FTId=PRO_0000056498. FT NP_BIND 244 249 NAD (By similarity). FT ACT_SITE 266 266 Proton acceptor (By similarity). FT ACT_SITE 300 300 Nucleophile (By similarity). FT SITE 165 165 Transition state stabilizer (By FT similarity). 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 //