AL2C4_ARATH
ID AL2C4_ARATH Reviewed; 501 AA.
AC Q56YU0; Q9LV57;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Aldehyde dehydrogenase family 2 member C4;
DE EC=1.2.1.3;
DE AltName: Full=ALDH1a;
DE AltName: Full=Protein REDUCED EPIDERMAL FLUORESCENCE 1;
GN Name=ALDH2C4; Synonyms=REF1; OrderedLocusNames=At3g24503; ORFNames=MOB24.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=11999848; DOI=10.1023/a:1014870429630;
RA Skibbe D.S., Liu F., Wen T.-J., Yandeau M.D., Cui X., Cao J., Simmons C.R.,
RA Schnable P.S.;
RT "Characterization of the aldehyde dehydrogenase gene families of Zea mays
RT and Arabidopsis.";
RL Plant Mol. Biol. 48:751-764(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 322-501.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND MUTAGENESIS OF GLY-152 AND GLY-416.
RX PubMed=14729911; DOI=10.1105/tpc.017509;
RA Nair R.B., Bastress K.L., Ruegger M.O., Denault J.W., Chapple C.;
RT "The Arabidopsis thaliana REDUCED EPIDERMAL FLUORESCENCE1 gene encodes an
RT aldehyde dehydrogenase involved in ferulic acid and sinapic acid
RT biosynthesis.";
RL Plant Cell 16:544-554(2004).
RN [7]
RP NOMENCLATURE.
RX PubMed=15358267; DOI=10.1016/j.tplants.2004.06.004;
RA Kirch H.-H., Bartels D., Wei Y., Schnable P.S., Wood A.J.;
RT "The ALDH gene superfamily of Arabidopsis.";
RL Trends Plant Sci. 9:371-377(2004).
CC -!- FUNCTION: Involved in ferulic acid and sinapic acid biosynthesis by
CC oxidation of conyferylaldehyde and sinapaldehyde, respectively. Can
CC oxidize L-lactaldehyde. Possesses activity on acetaldehyde and
CC glycolaldehyde in vitro. {ECO:0000269|PubMed:11999848,
CC ECO:0000269|PubMed:14729911}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF349448; AAM27004.1; -; mRNA.
DR EMBL; AB020746; BAB01998.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76907.1; -; Genomic_DNA.
DR EMBL; AY056398; AAL08254.1; -; mRNA.
DR EMBL; AK221230; BAD93825.1; -; mRNA.
DR RefSeq; NP_566749.1; NM_113359.4.
DR AlphaFoldDB; Q56YU0; -.
DR SMR; Q56YU0; -.
DR BioGRID; 7373; 3.
DR IntAct; Q56YU0; 1.
DR STRING; 3702.AT3G24503.1; -.
DR iPTMnet; Q56YU0; -.
DR MetOSite; Q56YU0; -.
DR PaxDb; Q56YU0; -.
DR PRIDE; Q56YU0; -.
DR ProteomicsDB; 244722; -.
DR EnsemblPlants; AT3G24503.1; AT3G24503.1; AT3G24503.
DR GeneID; 822042; -.
DR Gramene; AT3G24503.1; AT3G24503.1; AT3G24503.
DR KEGG; ath:AT3G24503; -.
DR Araport; AT3G24503; -.
DR TAIR; locus:505006369; AT3G24503.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_0_1; -.
DR InParanoid; Q56YU0; -.
DR OMA; RKAFEKW; -.
DR OrthoDB; 153834at2759; -.
DR PhylomeDB; Q56YU0; -.
DR PRO; PR:Q56YU0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q56YU0; baseline and differential.
DR Genevisible; Q56YU0; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISS:TAIR.
DR GO; GO:0050269; F:coniferyl-aldehyde dehydrogenase activity; IDA:TAIR.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IDA:TAIR.
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; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..501
FT /note="Aldehyde dehydrogenase family 2 member C4"
FT /id="PRO_0000256058"
FT ACT_SITE 268
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 302
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 245..250
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 169
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MUTAGEN 152
FT /note="G->E: In ref1-7; reduced activity on sinapaldehyde."
FT /evidence="ECO:0000269|PubMed:14729911"
FT MUTAGEN 416
FT /note="G->R: In ref1-6; reduced activity on sinapaldehyde."
FT /evidence="ECO:0000269|PubMed:14729911"
SQ SEQUENCE 501 AA; 54360 MW; 3E93A166B1D3ECF6 CRC64;
MENGKCNGAT TVKLPEIKFT KLFINGQFID AASGKTFETI DPRNGEVIAT IAEGDKEDVD
LAVNAARYAF DHGPWPRMTG FERAKLINKF ADLIEENIEE LAKLDAVDGG KLFQLGKYAD
IPATAGHFRY NAGAADKIHG ETLKMTRQSL FGYTLKEPIG VVGNIIPWNF PSIMFATKVA
PAMAAGCTMV VKPAEQTSLS ALFYAHLSKE AGIPDGVLNI VTGFGSTAGA AIASHMDVDK
VSFTGSTDVG RKIMQAAAAS NLKKVSLELG GKSPLLIFND ADIDKAADLA LLGCFYNKGE
ICVASSRVFV QEGIYDKVVE KLVEKAKDWT VGDPFDSTAR QGPQVDKRQF EKILSYIEHG
KNEGATLLTG GKAIGDKGYF IQPTIFADVT EDMKIYQDEI FGPVMSLMKF KTVEEGIKCA
NNTKYGLAAG ILSQDIDLIN TVSRSIKAGI IWVNCYFGFD LDCPYGGYKM SGNCRESGMD
ALDNYLQTKS VVMPLHNSPW M
