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Database: UniProt/SWISS-PROT
Entry: AL2B4_ARATH
LinkDB: AL2B4_ARATH
Original site: 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   25-APR-2018, entry version 126.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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
RT   novel 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.,
RA   Simmons C.R., Schnable P.S.;
RT   "Characterization of the aldehyde dehydrogenase gene families of Zea
RT   mays 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.,
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   [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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RP   AFTER 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: An aldehyde + NAD(+) + H(2)O = a carboxylate +
CC       NADH.
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}.
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   UniGene; At.22890; -.
DR   ProteinModelPortal; Q9SU63; -.
DR   SMR; Q9SU63; -.
DR   BioGrid; 9274; 2.
DR   STRING; 3702.AT3G48000.1; -.
DR   PaxDb; Q9SU63; -.
DR   PRIDE; Q9SU63; -.
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   eggNOG; COG1012; LUCA.
DR   HOGENOM; HOG000271505; -.
DR   InParanoid; Q9SU63; -.
DR   KO; K00128; -.
DR   OMA; TFVQEDV; -.
DR   OrthoDB; EOG0936062U; -.
DR   PhylomeDB; Q9SU63; -.
DR   BioCyc; ARA:AT3G48000-MONOMER; -.
DR   Reactome; R-ATH-380612; Metabolism of serotonin.
DR   Reactome; R-ATH-5365859; RA biosynthesis pathway.
DR   Reactome; R-ATH-70350; Fructose catabolism.
DR   Reactome; R-ATH-71384; Ethanol oxidation.
DR   PRO; PR:Q9SU63; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SU63; baseline and differential.
DR   Genevisible; Q9SU63; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; ISS:TAIR.
DR   GO; GO:0005524; F:ATP binding; IDA:TAIR.
DR   GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 2.
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   Complete proteome; Mitochondrion; NAD; Oxidoreductase;
KW   Reference proteome; Transit peptide.
FT   TRANSIT       1     38       Mitochondrion.
FT                                {ECO:0000269|PubMed:25732537}.
FT   CHAIN        39    538       Aldehyde dehydrogenase family 2 member
FT                                B4, mitochondrial.
FT                                /FTId=PRO_0000256056.
FT   NP_BIND     282    287       NAD. {ECO:0000250}.
FT   ACT_SITE    305    305       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10007, ECO:0000255|PROSITE-
FT                                ProRule:PRU10008}.
FT   ACT_SITE    339    339       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10007, ECO:0000255|PROSITE-
FT                                ProRule:PRU10008}.
FT   SITE        206    206       Transition state stabilizer.
FT                                {ECO:0000250}.
FT   CONFLICT    125    125       L -> C (in Ref. 6; CAA81249).
FT                                {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
//
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