AL221_ARATH
ID AL221_ARATH Reviewed; 596 AA.
AC Q0WSF1; Q70E95; Q9C837;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Aldehyde dehydrogenase 22A1;
DE EC=1.2.1.3;
DE AltName: Full=Novel aldehyde dehydrogenase family 22 member A1;
DE Flags: Precursor;
GN Name=ALDH22A1; OrderedLocusNames=At3g66658; ORFNames=T8E24.4;
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], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15830124; DOI=10.1007/s11103-004-7796-6;
RA Kirch H.-H., Schlingensiepen S., Kotchoni S., Sunkar R., Bartels D.;
RT "Detailed expression analysis of selected genes of the aldehyde
RT dehydrogenase(ALDH) gene superfamily in Arabidopsis thaliana.";
RL Plant Mol. Biol. 57:315-332(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 -!- 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q0WSF1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Constituively expressed at low levels.
CC {ECO:0000269|PubMed:15830124}.
CC -!- INDUCTION: Not induced by abscisic acid (ABA), dehydration and salt
CC stress. {ECO:0000269|PubMed:15830124}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50992.1; Type=Erroneous gene model prediction; Evidence={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; AJ584646; CAE48165.1; -; mRNA.
DR EMBL; AC036106; AAG50992.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74433.1; -; Genomic_DNA.
DR EMBL; AK227981; BAE99947.1; -; mRNA.
DR RefSeq; NP_974242.1; NM_202513.3. [Q0WSF1-1]
DR AlphaFoldDB; Q0WSF1; -.
DR SMR; Q0WSF1; -.
DR STRING; 3702.AT3G66658.2; -.
DR iPTMnet; Q0WSF1; -.
DR PaxDb; Q0WSF1; -.
DR PRIDE; Q0WSF1; -.
DR ProteomicsDB; 244892; -. [Q0WSF1-1]
DR EnsemblPlants; AT3G66658.2; AT3G66658.2; AT3G66658. [Q0WSF1-1]
DR GeneID; 819849; -.
DR Gramene; AT3G66658.2; AT3G66658.2; AT3G66658. [Q0WSF1-1]
DR KEGG; ath:AT3G66658; -.
DR Araport; AT3G66658; -.
DR TAIR; locus:2103425; AT3G66658.
DR eggNOG; KOG2454; Eukaryota.
DR InParanoid; Q0WSF1; -.
DR OrthoDB; 398557at2759; -.
DR PhylomeDB; Q0WSF1; -.
DR BioCyc; ARA:AT3G66658-MON; -.
DR PRO; PR:Q0WSF1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WSF1; baseline and differential.
DR Genevisible; Q0WSF1; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
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; 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 2: Evidence at transcript level;
KW Alternative splicing; NAD; Oxidoreductase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..596
FT /note="Aldehyde dehydrogenase 22A1"
FT /id="PRO_0000256069"
FT ACT_SITE 298
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 332
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 276..281
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 199
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 33
FT /note="V -> A (in Ref. 4; BAE99947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 596 AA; 66003 MW; 25AC39BC26E4C1A8 CRC64;
MPFWWPLIVL AFAYAICKFL LMLIPPNVPS IDVDASDVLA HGKDTEENSF IYIPPRGRSQ
QSDKKVQCYE PATMKYLGYF PALSPTEVEE RVTLSRKAQK TWAQSSFKLR RQFLRILLKY
IIEHQELICE VSSRDTGKTM VDASLGEIMT TCEKITWLLS EGERWLKPES RSSGRAMLHK
VSRVEFHPLG VIGAIVPWNY PFHNIFNPML AAVFSGNGIV IKVSEHASWS GCFYFRIIQA
ALAAVGAPEN LVDVITGFAE TGEALVSSVD KMIFVGSTAV GKMIMRNAAE TLTPVTLELG
GKDAFIICED ADVSHVAQVA VRGTLQSSGQ NCAGAERFYV HKDIYTAFIG QVTKIVKSVS
AGPPLTGRYD MGAICLQEHS EHLQSLVNDA LDKGAEIAVR GSFGHLGEDA VDQYFPPTVL
INVNHNMKIM KEEAFGPIMP IMQFSTDEEV IKLANDSRYA LGCAVFSGSK HRAKQIASQI
QCGVAAINDF ASNYMCQSLP FGGVKDSGFG RFAGIEGLRA CCLVKSVVED RFWPLIKTKI
PKPIQYPVAE NAFEFQEALV ETLYGLNIWD RLRSLIDVLK FLTDQSSNVS RTRKSH
