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   16-JUN-2009, entry version 26.
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; 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   MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   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.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   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
RT   thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
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.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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: An aldehyde + NAD(+) + H(2)O = an acid + NADH.
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential).
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   -!- INDUCTION: Not induced by abscisic acid (ABA), dehydration and
CC       salt stress.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG50992.1; Type=Erroneous gene model prediction;
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DR   EMBL; AJ584646; CAE48165.1; -; mRNA.
DR   EMBL; AC036106; AAG50992.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK227981; BAE99947.1; -; mRNA.
DR   IPI; IPI00526692; -.
DR   RefSeq; NP_974242.1; -.
DR   UniGene; At.43176; -.
DR   HSSP; P11883; 1AD3.
DR   PRIDE; Q0WSF1; -.
DR   GeneID; 819849; -.
DR   GenomeReviews; BA000014_GR; AT3G66658.
DR   NMPDR; fig|3702.1.peg.12680; -.
DR   TAIR; At3g66658; -.
DR   OMA; Q0WSF1; SWNYPFH.
DR   BRENDA; 1.2.1.3; 302.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH.
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; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Complete proteome; NAD; Oxidoreductase;
KW   Secreted; Signal.
FT   SIGNAL        1     30       Potential.
FT   CHAIN        31    596       Aldehyde dehydrogenase 22A1.
FT                                /FTId=PRO_0000256069.
FT   NP_BIND     276    281       NAD (By similarity).
FT   ACT_SITE    298    298       Proton acceptor (By similarity).
FT   ACT_SITE    332    332       Nucleophile (By similarity).
FT   SITE        199    199       Transition state stabilizer (By
FT                                similarity).
FT   CONFLICT     33     33       V -> A (in Ref. 3; BAE99947).
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
//