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   27-MAR-2024, entry version 113.
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};
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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.Q0WSF1; -.
DR   iPTMnet; Q0WSF1; -.
DR   PaxDb; 3702-AT3G66658-2; -.
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; AT3G66658; ALDH22A1.
DR   eggNOG; KOG2454; Eukaryota.
DR   InParanoid; Q0WSF1; -.
DR   OrthoDB; 3078548at2759; -.
DR   PhylomeDB; Q0WSF1; -.
DR   BioCyc; ARA:AT3G66658-MONOMER; -.
DR   PRO; PR:Q0WSF1; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q0WSF1; baseline and differential.
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; IEA:UniProtKB-EC.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   CDD; cd07098; ALDH_F15-22; 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   PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR   PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
DR   Genevisible; Q0WSF1; AT.
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
//