GenomeNet

Database: UniProt/SWISS-PROT
Entry: AL2B7_ARATH
LinkDB: AL2B7_ARATH
Original site: 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   13-FEB-2019, entry version 123.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
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   [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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   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
RT   reference 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.,
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE
RP   AFTER 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(+) +
CC         NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067,
CC         ChEBI:CHEBI:57540, 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; Positions=303, 309; Evidence={ECO:0000305};
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   UniGene; At.22317; -.
DR   ProteinModelPortal; Q8S528; -.
DR   SMR; Q8S528; -.
DR   STRING; 3702.AT1G23800.1; -.
DR   PaxDb; Q8S528; -.
DR   PRIDE; Q8S528; -.
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   eggNOG; COG1012; LUCA.
DR   HOGENOM; HOG000271505; -.
DR   InParanoid; Q8S528; -.
DR   KO; K00128; -.
DR   OMA; GEKLDWP; -.
DR   OrthoDB; 153834at2759; -.
DR   PhylomeDB; Q8S528; -.
DR   BioCyc; ARA:AT1G23800-MONOMER; -.
DR   Reactome; R-ATH-5365859; RA biosynthesis pathway.
DR   Reactome; R-ATH-71384; Ethanol oxidation.
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: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   Complete proteome; Mitochondrion; NAD; Oxidoreductase;
KW   Reference proteome; Transit peptide.
FT   TRANSIT       1     34       Mitochondrion.
FT                                {ECO:0000269|PubMed:25732537}.
FT   CHAIN        35    534       Aldehyde dehydrogenase family 2 member
FT                                B7, mitochondrial.
FT                                /FTId=PRO_0000256057.
FT   NP_BIND     278    283       NAD. {ECO:0000250}.
FT   ACT_SITE    301    301       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10007, ECO:0000255|PROSITE-
FT                                ProRule:PRU10008}.
FT   ACT_SITE    335    335       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10007, ECO:0000255|PROSITE-
FT                                ProRule:PRU10008}.
FT   SITE        202    202       Transition state stabilizer.
FT                                {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
//
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