ID   AL2B4_ARATH             Reviewed;         538 AA.
AC   Q9SU63; Q42090;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Aldehyde dehydrogenase family 2 member B4, mitochondrial;
DE            Short=ALDH2a;
DE            EC=1.2.1.3;
DE   Flags: Precursor;
GN   Name=ALDH2B4; Synonyms=ALDH2; OrderedLocusNames=At3g48000;
GN   ORFNames=T17F15.130;
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].
RX   PubMed=10831839; DOI=10.1016/s0378-1119(00)00152-9;
RA   Li Y., Nakazono M., Tsutsumi N., Hirai A.;
RT   "Molecular and cellular characterizations of a cDNA clone encoding a novel
RT   isozyme of aldehyde dehydrogenase from rice.";
RL   Gene 249:67-74(2000).
RN   [2]
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   [3]
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   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 9-125.
RA   Philipps G., Gigot C.;
RT   "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL   Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP   PHE-38.
RX   PubMed=25732537; DOI=10.1093/jxb/erv064;
RA   Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT   "Identification of cleavage sites and substrate proteins for two
RT   mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL   J. Exp. Bot. 66:2691-2708(2015).
CC   -!- FUNCTION: Possesses activity on acetaldehyde and glycolaldehyde in
CC       vitro. {ECO:0000269|PubMed:11999848}.
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: Mitochondrion matrix
CC       {ECO:0000305|PubMed:25732537}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AB030820; BAA96792.1; -; mRNA.
DR   EMBL; AF349447; AAM27003.1; -; mRNA.
DR   EMBL; AL049658; CAB41139.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78355.1; -; Genomic_DNA.
DR   EMBL; AF327426; AAG42016.1; -; mRNA.
DR   EMBL; AF349522; AAK15569.1; -; mRNA.
DR   EMBL; AF372911; AAK49627.1; -; mRNA.
DR   EMBL; AY090443; AAL91287.1; -; mRNA.
DR   EMBL; BT000752; AAN31892.1; -; mRNA.
DR   EMBL; BT006371; AAP21179.1; -; mRNA.
DR   EMBL; Z26417; CAA81249.1; -; mRNA.
DR   PIR; T06683; T06683.
DR   RefSeq; NP_190383.1; NM_114669.4.
DR   AlphaFoldDB; Q9SU63; -.
DR   SMR; Q9SU63; -.
DR   BioGRID; 9274; 4.
DR   STRING; 3702.Q9SU63; -.
DR   PaxDb; 3702-AT3G48000-1; -.
DR   ProteomicsDB; 244707; -.
DR   EnsemblPlants; AT3G48000.1; AT3G48000.1; AT3G48000.
DR   GeneID; 823955; -.
DR   Gramene; AT3G48000.1; AT3G48000.1; AT3G48000.
DR   KEGG; ath:AT3G48000; -.
DR   Araport; AT3G48000; -.
DR   TAIR; AT3G48000; ALDH2B4.
DR   eggNOG; KOG2450; Eukaryota.
DR   HOGENOM; CLU_005391_0_1_1; -.
DR   InParanoid; Q9SU63; -.
DR   OMA; WSNTFNK; -.
DR   OrthoDB; 3078548at2759; -.
DR   PhylomeDB; Q9SU63; -.
DR   BioCyc; ARA:AT3G48000-MONOMER; -.
DR   PRO; PR:Q9SU63; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SU63; baseline and differential.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISS:TAIR.
DR   GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   CDD; cd07142; ALDH_F2BC; 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:SF225; ALDEHYDE DEHYDROGENASE FAMILY 2 MEMBER B4, MITOCHONDRIAL; 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; Q9SU63; AT.
PE   1: Evidence at protein level;
KW   Mitochondrion; NAD; Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT         1..38
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:25732537"
FT   CHAIN           39..538
FT                   /note="Aldehyde dehydrogenase family 2 member B4,
FT                   mitochondrial"
FT                   /id="PRO_0000256056"
FT   ACT_SITE        305
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        339
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         282..287
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            206
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        125
FT                   /note="L -> C (in Ref. 6; CAA81249)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   538 AA;  58589 MW;  B7C054157659391C CRC64;
     MAARRVSSLL SRSFSASSPL LFRSQGRNCY NGGILRRFGT SSAAAEEIIN PSVQVSHTQL
     LINGNFVDSA SGKTFPTLDP RTGEVIAHVA EGDAEDINRA VKAARTAFDE GPWPKMSAYE
     RSRVLLRFAD LVEKHSEELA SLETWDNGKP YQQSLTAEIP MFARLFRYYA GWADKIHGLT
     IPADGNYQVH TLHEPIGVAG QIIPWNFPLL MFAWKVGPAL ACGNTIVLKT AEQTPLTAFY
     AGKLFLEAGL PPGVLNIVSG FGATAGAALA SHMDVDKLAF TGSTDTGKVI LGLAANSNLK
     PVTLELGGKS PFIVFEDADI DKAVELAHFA LFFNQGQCCC AGSRTFVHEK VYDEFVEKSK
     ARALKRVVGD PFRKGIEQGP QIDLKQFEKV MKYIKSGIES NATLECGGDQ IGDKGYFIQP
     TVFSNVKDDM LIAQDEIFGP VQSILKFSDV DEVIKRANET KYGLAAGVFT KNLDTANRVS
     RALKAGTVWV NCFDVFDAAI PFGGYKMSGN GREKGIYSLN NYLQIKAVVT ALNKPAWI
//