ID   AL7B4_ARATH             Reviewed;         508 AA.
AC   Q9SYG7; Q546B7;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-NOV-2002, sequence version 3.
DT   24-JAN-2024, entry version 150.
DE   RecName: Full=Aldehyde dehydrogenase family 7 member B4;
DE            EC=1.2.1.3;
DE   AltName: Full=Antiquitin-1;
DE   AltName: Full=Turgor-responsive ALDH;
GN   Name=ALDH7B4; OrderedLocusNames=At1g54100; ORFNames=F15I1.19;
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 {ECO:0000312|EMBL:AAD25783.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX   PubMed=15830124; DOI=10.1007/s11103-004-7796-6;
RA   Kirch H.-H., Schlingensiepen S., Kotchoni S., Sunkar R., Bartels D.;
RT   "Detailed expression analysis of selected genes of the aldehyde
RT   dehydrogenase(ALDH) gene superfamily in Arabidopsis thaliana.";
RL   Plant Mol. Biol. 57:315-332(2005).
RN   [2] {ECO:0000305}
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] {ECO:0000305}
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] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NOMENCLATURE.
RX   PubMed=15358267; DOI=10.1016/j.tplants.2004.06.004;
RA   Kirch H.-H., Bartels D., Wei Y., Schnable P.S., Wood A.J.;
RT   "The ALDH gene superfamily of Arabidopsis.";
RL   Trends Plant Sci. 9:371-377(2004).
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|UniProtKB:P83402}.
CC   -!- INDUCTION: By abscisic acid (ABA) and dehydration in roots and
CC       plantlets, and by salt stress in plantlets.
CC       {ECO:0000269|PubMed:15830124}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ584645; CAE48164.1; -; mRNA.
DR   EMBL; AC006577; AAD25783.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33048.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33049.1; -; Genomic_DNA.
DR   EMBL; AY048242; AAK82504.1; -; mRNA.
DR   EMBL; AF378873; AAK55676.1; -; mRNA.
DR   EMBL; AY091032; AAM13853.1; -; mRNA.
DR   EMBL; AY102145; AAM26712.1; -; mRNA.
DR   EMBL; AY117345; AAM51420.1; -; mRNA.
DR   EMBL; AK230363; BAF02162.1; -; mRNA.
DR   PIR; H96581; H96581.
DR   RefSeq; NP_175812.1; NM_104287.5.
DR   RefSeq; NP_849807.1; NM_179476.3.
DR   AlphaFoldDB; Q9SYG7; -.
DR   SMR; Q9SYG7; -.
DR   BioGRID; 27074; 2.
DR   STRING; 3702.Q9SYG7; -.
DR   PaxDb; 3702-AT1G54100-1; -.
DR   ProteomicsDB; 244867; -.
DR   EnsemblPlants; AT1G54100.1; AT1G54100.1; AT1G54100.
DR   EnsemblPlants; AT1G54100.2; AT1G54100.2; AT1G54100.
DR   GeneID; 841849; -.
DR   Gramene; AT1G54100.1; AT1G54100.1; AT1G54100.
DR   Gramene; AT1G54100.2; AT1G54100.2; AT1G54100.
DR   KEGG; ath:AT1G54100; -.
DR   Araport; AT1G54100; -.
DR   TAIR; AT1G54100; ALDH7B4.
DR   eggNOG; KOG2453; Eukaryota.
DR   HOGENOM; CLU_005391_1_2_1; -.
DR   InParanoid; Q9SYG7; -.
DR   OMA; DAWKVYM; -.
DR   OrthoDB; 8449at2759; -.
DR   PhylomeDB; Q9SYG7; -.
DR   BioCyc; ARA:AT1G54100-MONOMER; -.
DR   PRO; PR:Q9SYG7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SYG7; baseline and differential.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; ISS:UniProtKB.
DR   GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR   GO; GO:0009269; P:response to desiccation; IEP:TAIR.
DR   GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR   CDD; cd07130; ALDH_F7_AASADH; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR044638; ALDH7A1-like.
DR   PANTHER; PTHR43521; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43521:SF1; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
DR   Genevisible; Q9SYG7; AT.
PE   2: Evidence at transcript level;
KW   NAD; Oxidoreductase; Reference proteome; Stress response.
FT   CHAIN           1..508
FT                   /note="Aldehyde dehydrogenase family 7 member B4"
FT                   /id="PRO_0000056495"
FT   ACT_SITE        266
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        300
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   BINDING         244..249
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            165
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   508 AA;  54208 MW;  7690BB8D906B263A CRC64;
     MGSANNEYEF LSEIGLTSHN LGSYVAGKWQ ANGPLVSTLN PANNQPIAQV VEASLEDYEQ
     GLKACEEAAK IWMQVTAPKR GDIVRQIGDA LRSKLDYLGR LLSLEMGKIL AEGIGEVQEV
     IDMCDFAVGL SRQLNGSVIP SERPNHMMLE MWNPLGIVGV ITAFNFPCAV LGWNACIALV
     CGNCVVWKGA PTTPLITIAM TKLVAEVLEK NNLPGAIFTA MCGGAEIGEA IAKDTRIPLV
     SFTGSSRVGS MVQQTVNARS GKTLLELSGN NAIIVMDDAD IQLAARSVLF AAVGTAGQRC
     TTCRRLLLHE SVYDKVLEQL LTSYKQVKIG NPLEKGTLLG PLHTPESKKN FEKGIEVIKS
     QGGKILTGGK AVEGEGNFVE PTIIEISADA AVVKEELFAP VLYVLKFKSF GEAVAINNSV
     PQGLSSSIFT RNPENIFRWI GPLGSDCGIV NVNIPTNGAE IGGAFGGEKA TGGGREAGSD
     SWKQYMRRST CTINYGNELP LAQGINFG
//