AL2B7_ARATH
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 03-AUG-2022, entry version 136.
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.AT1G23800.1; -.
DR PaxDb; Q8S528; -.
DR PRIDE; Q8S528; -.
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; locus:2034855; AT1G23800.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_1_1; -.
DR InParanoid; Q8S528; -.
DR OMA; VTGPGHT; -.
DR OrthoDB; 153834at2759; -.
DR PhylomeDB; Q8S528; -.
DR BioCyc; ARA:AT1G23800-MON; -.
DR PRO; PR:Q8S528; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8S528; baseline and differential.
DR Genevisible; Q8S528; AT.
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 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..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
