AL2B4_ARATH
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 03-AUG-2022, entry version 145.
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.AT3G48000.1; -.
DR PaxDb; Q9SU63; -.
DR PRIDE; Q9SU63; -.
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; locus:2097845; AT3G48000.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_1_1; -.
DR InParanoid; Q9SU63; -.
DR OMA; RRMDTGQ; -.
DR OrthoDB; 153834at2759; -.
DR PhylomeDB; Q9SU63; -.
DR BioCyc; ARA:AT3G48000-MON; -.
DR PRO; PR:Q9SU63; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SU63; baseline and differential.
DR Genevisible; Q9SU63; AT.
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 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 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
