ABA2_ARATH
ID ABA2_ARATH Reviewed; 285 AA.
AC Q9C826;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Xanthoxin dehydrogenase {ECO:0000305};
DE EC=1.1.1.288 {ECO:0000269|PubMed:12172025};
DE AltName: Full=Protein ABSCISIC ACID DEFICIENT 2 {ECO:0000303|PubMed:9159947};
DE AltName: Full=Protein GLUCOSE INSENSITIVE 1 {ECO:0000303|PubMed:9707641};
DE AltName: Full=Protein IMPAIRED SUCROSE INDUCTION 4 {ECO:0000303|PubMed:11439129};
DE AltName: Full=Protein SALOBRENO 3 {ECO:0000303|PubMed:12172025};
DE AltName: Full=Protein SALT RESISTANT 1 {ECO:0000303|PubMed:12172025};
DE AltName: Full=Protein SUGAR INSENSITIVE 4 {ECO:0000303|PubMed:10972885};
DE AltName: Full=Short-chain alcohol dehydrogenase ABA2 {ECO:0000303|PubMed:12172025};
DE AltName: Full=Short-chain dehydrogenase reductase 1 {ECO:0000303|PubMed:12417697};
DE Short=AtSDR1 {ECO:0000303|PubMed:12417697};
DE AltName: Full=Xanthoxin oxidase {ECO:0000303|PubMed:12172025};
GN Name=ABA2 {ECO:0000303|PubMed:9159947};
GN Synonyms=GIN1 {ECO:0000303|PubMed:9707641},
GN ISI4 {ECO:0000303|PubMed:11439129}, SAN3 {ECO:0000303|PubMed:12172025},
GN SDR1 {ECO:0000303|PubMed:12417697}, SIS4 {ECO:0000303|PubMed:10972885},
GN SRE1 {ECO:0000303|PubMed:12172025};
GN OrderedLocusNames=At1g52340 {ECO:0000312|Araport:AT1G52340};
GN ORFNames=F19K6.3 {ECO:0000312|EMBL:AAG51536.1};
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], MUTAGENESIS OF ALA-45; ARG-145;
RP GLY-162 AND SER-264, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION,
RP AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=12417697; DOI=10.1105/tpc.006494;
RA Cheng W.-H., Endo A., Zhou L., Penney J., Chen H.-C., Arroyo A., Leon P.,
RA Nambara E., Asami T., Seo M., Koshiba T., Sheen J.;
RT "A unique short-chain dehydrogenase/reductase in Arabidopsis glucose
RT signaling and abscisic acid biosynthesis and functions.";
RL Plant Cell 14:2723-2743(2002).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=9159947; DOI=10.1104/pp.114.1.161;
RA Schwartz S.H., Leon-Kloosterziel K.M., Koornneef M., Zeevaart J.A.;
RT "Biochemical characterization of the aba2 and aba3 mutants in Arabidopsis
RT thaliana.";
RL Plant Physiol. 114:161-166(1997).
RN [6]
RP IDENTIFICATION.
RX PubMed=9707641; DOI=10.1073/pnas.95.17.10294;
RA Zhou L., Jang J.-C., Jones T.L., Sheen J.;
RT "Glucose and ethylene signal transduction crosstalk revealed by an
RT Arabidopsis glucose-insensitive mutant.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10294-10299(1998).
RN [7]
RP FUNCTION.
RX PubMed=10972885; DOI=10.1046/j.1365-313x.2000.00833.x;
RA Laby R.J., Kincaid M.S., Kim D., Gibson S.I.;
RT "The Arabidopsis sugar-insensitive mutants sis4 and sis5 are defective in
RT abscisic acid synthesis and response.";
RL Plant J. 23:587-596(2000).
RN [8]
RP IDENTIFICATION, AND MUTAGENESIS OF ALA-236.
RC STRAIN=cv. Columbia;
RX PubMed=11439129; DOI=10.1046/j.1365-313x.2001.2641043.x;
RA Rook F., Corke F., Card R., Munz G., Smith C., Bevan M.W.;
RT "Impaired sucrose-induction mutants reveal the modulation of sugar-induced
RT starch biosynthetic gene expression by abscisic acid signalling.";
RL Plant J. 26:421-433(2001).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-28; SER-176 AND SER-264.
RC STRAIN=cv. Columbia;
RX PubMed=12172025; DOI=10.1105/tpc.002477;
RA Gonzalez-Guzman M., Apostolova N., Belles J.M., Barrero J.M., Piqueras P.,
RA Ponce M.R., Micol J.L., Serrano R., Rodriguez P.L.;
RT "The short-chain alcohol dehydrogenase ABA2 catalyzes the conversion of
RT xanthoxin to abscisic aldehyde.";
RL Plant Cell 14:1833-1846(2002).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Involved in the biosynthesis of abscisic acid
CC (PubMed:12172025, PubMed:12417697, PubMed:9159947, PubMed:10972885).
CC Catalyzes the conversion of xanthoxin to abscisic aldehyde
CC (PubMed:12417697, PubMed:9159947, PubMed:12172025).
CC {ECO:0000269|PubMed:10972885, ECO:0000269|PubMed:12172025,
CC ECO:0000269|PubMed:12417697, ECO:0000269|PubMed:9159947}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-cis,4-trans-xanthoxin + NAD(+) = 2-cis-(+)-abscisic aldehyde
CC + H(+) + NADH; Xref=Rhea:RHEA:12548, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31157, ChEBI:CHEBI:32304, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.1.1.288;
CC Evidence={ECO:0000269|PubMed:12172025};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12549;
CC Evidence={ECO:0000269|PubMed:12172025};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-trans,4-trans-xanthoxin + NAD(+) = 2-trans-(+)-abscisic
CC aldehyde + H(+) + NADH; Xref=Rhea:RHEA:49312, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:91126,
CC ChEBI:CHEBI:91130; Evidence={ECO:0000269|PubMed:12172025};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49313;
CC Evidence={ECO:0000269|PubMed:12172025};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19 uM for xanthoxin {ECO:0000269|PubMed:12172025};
CC KM=10 mM for 3,5,5'-trimethylcyclohexanol
CC {ECO:0000269|PubMed:12172025};
CC Note=no activity with xanthoxic acid, ethanol, isopropanol, butanol,
CC cyclohexanol and 2,6-dimethylcyclohexanol.;
CC -!- INTERACTION:
CC Q9C826; Q9C826: ABA2; NbExp=6; IntAct=EBI-4464299, EBI-4464299;
CC Q9C826; Q8H1R4: ABCI10; NbExp=3; IntAct=EBI-4464299, EBI-17091580;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12417697}.
CC -!- TISSUE SPECIFICITY: Predominantly in roots and stems, and at lower
CC levels in leaves and seeds. {ECO:0000269|PubMed:12172025,
CC ECO:0000269|PubMed:12417697}.
CC -!- INDUCTION: Constitutively expressed and not up regulated by osmotic
CC stress. {ECO:0000269|PubMed:12172025, ECO:0000269|PubMed:12417697,
CC ECO:0000269|PubMed:9159947}.
CC -!- MISCELLANEOUS: The biological substrate is probably 2-cis,4-trans-
CC xanthoxin.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AC037424; AAG51536.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32789.1; -; Genomic_DNA.
DR EMBL; BT003412; AAO30075.1; -; mRNA.
DR EMBL; AY099603; AAM20454.1; -; mRNA.
DR EMBL; AY082344; AAL99237.1; -; mRNA.
DR EMBL; AY082345; AAL99238.1; -; Genomic_DNA.
DR PIR; F96563; F96563.
DR RefSeq; NP_175644.1; NM_104113.5.
DR AlphaFoldDB; Q9C826; -.
DR SMR; Q9C826; -.
DR BioGRID; 26890; 4.
DR IntAct; Q9C826; 3.
DR STRING; 3702.AT1G52340.1; -.
DR SwissLipids; SLP:000001503; -.
DR iPTMnet; Q9C826; -.
DR PaxDb; Q9C826; -.
DR PRIDE; Q9C826; -.
DR ProteomicsDB; 244603; -.
DR EnsemblPlants; AT1G52340.1; AT1G52340.1; AT1G52340.
DR GeneID; 841665; -.
DR Gramene; AT1G52340.1; AT1G52340.1; AT1G52340.
DR KEGG; ath:AT1G52340; -.
DR Araport; AT1G52340; -.
DR TAIR; locus:2018149; AT1G52340.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_0_1; -.
DR InParanoid; Q9C826; -.
DR OMA; VYLCCKA; -.
DR OrthoDB; 1053465at2759; -.
DR PhylomeDB; Q9C826; -.
DR BioCyc; ARA:AT1G52340-MON; -.
DR BioCyc; MetaCyc:AT1G52340-MON; -.
DR BRENDA; 1.1.1.288; 399.
DR SABIO-RK; Q9C826; -.
DR PRO; PR:Q9C826; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C826; baseline and differential.
DR Genevisible; Q9C826; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0010301; F:xanthoxin dehydrogenase activity; IDA:TAIR.
DR GO; GO:0009688; P:abscisic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0006561; P:proline biosynthetic process; IMP:TAIR.
DR GO; GO:0010115; P:regulation of abscisic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0009750; P:response to fructose; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0010182; P:sugar mediated signaling pathway; TAS:TAIR.
DR CDD; cd05326; secoisolariciresinol-DH_like_SDR_c; 1.
DR InterPro; IPR045309; ABA2-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Abscisic acid biosynthesis; Acetylation; Cytoplasm; NAD; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..285
FT /note="Xanthoxin dehydrogenase"
FT /id="PRO_0000282347"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 28
FT /note="G->R: In aba2-12/sre1-2; reduced absicic acid
FT synthesis."
FT /evidence="ECO:0000269|PubMed:12172025"
FT MUTAGEN 45
FT /note="A->V: In aba2-4/sis4-2; reduced absicic acid
FT synthesis."
FT /evidence="ECO:0000269|PubMed:12417697"
FT MUTAGEN 145
FT /note="R->C: In gin1-2; reduced absicic acid synthesis."
FT /evidence="ECO:0000269|PubMed:12417697"
FT MUTAGEN 162
FT /note="G->R: In aba2-3/sis4-1; reduced absicic acid
FT synthesis."
FT /evidence="ECO:0000269|PubMed:12417697"
FT MUTAGEN 176
FT /note="S->F: In aba2-13/san3-1; reduced absicic acid
FT synthesis."
FT /evidence="ECO:0000269|PubMed:12172025"
FT MUTAGEN 236
FT /note="A->V: In isi4; reduced absicic acid synthesis."
FT /evidence="ECO:0000269|PubMed:11439129"
FT MUTAGEN 264
FT /note="S->N: In aba2-1; reduced absicic acid synthesis."
FT /evidence="ECO:0000269|PubMed:12172025,
FT ECO:0000269|PubMed:12417697"
SQ SEQUENCE 285 AA; 30272 MW; 8B555DAED7386DF4 CRC64;
MSTNTESSSY SSLPSQRLLG KVALITGGAT GIGESIVRLF HKHGAKVCIV DLQDDLGGEV
CKSLLRGESK ETAFFIHGDV RVEDDISNAV DFAVKNFGTL DILINNAGLC GAPCPDIRNY
SLSEFEMTFD VNVKGAFLSM KHAARVMIPE KKGSIVSLCS VGGVVGGVGP HSYVGSKHAV
LGLTRSVAAE LGQHGIRVNC VSPYAVATKL ALAHLPEEER TEDAFVGFRN FAAANANLKG
VELTVDDVAN AVLFLASDDS RYISGDNLMI DGGFTCTNHS FKVFR
