ID   AL2B7_ARATH             Reviewed;         534 AA.
AC   Q8S528; Q94C67; Q9ZUB6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Aldehyde dehydrogenase family 2 member B7, mitochondrial;
DE            Short=ALDH2b;
DE            EC=1.2.1.3;
DE   Flags: Precursor;
GN   Name=ALDH2B7; Synonyms=ALDH3; OrderedLocusNames=At1g23800;
GN   ORFNames=F5O8.33, F5O8.35;
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], 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP   TYR-34.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC98035.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAL99612.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF348416; AAL99612.1; ALT_FRAME; mRNA.
DR   EMBL; AC005990; AAC98035.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE30433.1; -; Genomic_DNA.
DR   EMBL; AY035139; AAK59643.1; -; mRNA.
DR   EMBL; AY113912; AAM44960.1; -; mRNA.
DR   PIR; C86372; C86372.
DR   RefSeq; NP_564204.1; NM_102228.4.
DR   AlphaFoldDB; Q8S528; -.
DR   SMR; Q8S528; -.
DR   BioGRID; 24229; 2.
DR   STRING; 3702.Q8S528; -.
DR   PaxDb; 3702-AT1G23800-1; -.
DR   ProteomicsDB; 244825; -.
DR   EnsemblPlants; AT1G23800.1; AT1G23800.1; AT1G23800.
DR   GeneID; 838991; -.
DR   Gramene; AT1G23800.1; AT1G23800.1; AT1G23800.
DR   KEGG; ath:AT1G23800; -.
DR   Araport; AT1G23800; -.
DR   TAIR; AT1G23800; ALDH2B7.
DR   eggNOG; KOG2450; Eukaryota.
DR   HOGENOM; CLU_005391_0_1_1; -.
DR   InParanoid; Q8S528; -.
DR   OMA; ILMGAWK; -.
DR   OrthoDB; 3078548at2759; -.
DR   PhylomeDB; Q8S528; -.
DR   BioCyc; ARA:AT1G23800-MONOMER; -.
DR   PRO; PR:Q8S528; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8S528; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISS: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: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; Q8S528; AT.
PE   1: Evidence at protein level;
KW   Mitochondrion; NAD; Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT         1..34
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:25732537"
FT   CHAIN           35..534
FT                   /note="Aldehyde dehydrogenase family 2 member B7,
FT                   mitochondrial"
FT                   /id="PRO_0000256057"
FT   ACT_SITE        301
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        335
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         278..283
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            202
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   534 AA;  58153 MW;  C709B0E539E52C31 CRC64;
     MASRRVSSLL SRSFMSSSRS IFSLRGMNRG AQRYSNLAAA VENTITPPVK VEHTQLLIGG
     RFVDAVSGKT FPTLDPRNGE VIAQVSEGDA EDVNRAVAAA RKAFDEGPWP KMTAYERSKI
     LFRFADLIEK HNDEIAALET WDNGKPYEQS AQIEVPMLAR VFRYYAGWAD KIHGMTMPGD
     GPHHVQTLHE PIGVAGQIIP WNFPLLMLSW KLGPALACGN TVVLKTAEQT PLSALLVGKL
     LHEAGLPDGV VNIVSGFGAT AGAAIASHMD VDKVAFTGST DVGKIILELA SKSNLKAVTL
     ELGGKSPFIV CEDADVDQAV ELAHFALFFN QGQCCCAGSR TFVHERVYDE FVEKAKARAL
     KRNVGDPFKS GIEQGPQVDS EQFNKILKYI KHGVEAGATL QAGGDRLGSK GYYIQPTVFS
     DVKDDMLIAT DEIFGPVQTI LKFKDLDEVI ARANNSRYGL AAGVFTQNLD TAHRLMRALR
     VGTVWINCFD VLDASIPFGG YKMSGIGREK GIYSLNNYLQ VKAVVTSLKN PAWL
//