ID SSDH_ARATH Reviewed; 528 AA.
AC Q9SAK4; Q9SEK4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 24-JAN-2024, entry version 150.
DE RecName: Full=Succinate-semialdehyde dehydrogenase, mitochondrial {ECO:0000303|PubMed:10517851};
DE Short=At-SSADH1 {ECO:0000303|PubMed:10517851};
DE EC=1.2.1.24 {ECO:0000269|PubMed:10517851};
DE AltName: Full=Aldehyde dehydrogenase family 5 member F1 {ECO:0000303|PubMed:15358267, ECO:0000303|PubMed:22639603};
DE AltName: Full=NAD(+)-dependent succinic semialdehyde dehydrogenase {ECO:0000303|PubMed:10517851};
DE AltName: Full=Protein ENLARGED FIL EXPRESSING DOMAIN 1 {ECO:0000303|PubMed:21690177, ECO:0000303|PubMed:25840087};
DE Flags: Precursor;
GN Name=ALDH5F1 {ECO:0000303|PubMed:15358267, ECO:0000303|PubMed:22639603};
GN Synonyms=ENF1 {ECO:0000303|PubMed:21690177, ECO:0000303|PubMed:25840087},
GN SSADH1 {ECO:0000303|PubMed:10517851};
GN OrderedLocusNames=At1g79440 {ECO:0000312|Araport:AT1G79440};
GN ORFNames=T8K14.14 {ECO:0000312|EMBL:AAD30232.1};
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 [MRNA], FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=10517851; DOI=10.1104/pp.121.2.589;
RA Busch K.B., Fromm H.;
RT "Plant succinic semialdehyde dehydrogenase. Cloning, purification,
RT localization in mitochondria, and regulation by adenine nucleotides.";
RL Plant Physiol. 121:589-597(1999).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12740438; DOI=10.1073/pnas.1037532100;
RA Bouche N., Fait A., Bouchez D., Moeller S.G., Fromm H.;
RT "Mitochondrial succinic-semialdehyde dehydrogenase of the gamma-
RT aminobutyrate shunt is required to restrict levels of reactive oxygen
RT intermediates in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:6843-6848(2003).
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).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=15642352; DOI=10.1016/j.febslet.2004.12.004;
RA Fait A., Yellin A., Fromm H.;
RT "GABA shunt deficiencies and accumulation of reactive oxygen intermediates:
RT insight from Arabidopsis mutants.";
RL FEBS Lett. 579:415-420(2005).
RN [8]
RP INDUCTION BY COLD.
RX PubMed=17461790; DOI=10.1111/j.1365-313x.2007.03100.x;
RA Kaplan F., Kopka J., Sung D.Y., Zhao W., Popp M., Porat R., Guy C.L.;
RT "Transcript and metabolite profiling during cold acclimation of Arabidopsis
RT reveals an intricate relationship of cold-regulated gene expression with
RT modifications in metabolite content.";
RL Plant J. 50:967-981(2007).
RN [9]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18846220; DOI=10.1371/journal.pone.0003383;
RA Ludewig F., Hueser A., Fromm H., Beauclair L., Bouche N.;
RT "Mutants of GABA transaminase (POP2) suppress the severe phenotype of
RT succinic semialdehyde dehydrogenase (ssadh) mutants in Arabidopsis.";
RL PLoS ONE 3:E3383-E3383(2008).
RN [10]
RP INDUCTION BY SALT.
RX PubMed=20122158; DOI=10.1186/1471-2229-10-20;
RA Renault H., Roussel V., El Amrani A., Arzel M., Renault D., Bouchereau A.,
RA Deleu C.;
RT "The Arabidopsis pop2-1 mutant reveals the involvement of GABA transaminase
RT in salt stress tolerance.";
RL BMC Plant Biol. 10:20-20(2010).
RN [11]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=22639603; DOI=10.3389/fpls.2011.00065;
RA Stiti N., Missihoun T.D., Kotchoni S.O., Kirch H.-H., Bartels D.;
RT "Aldehyde dehydrogenases in Arabidopsis thaliana: Biochemical requirements,
RT metabolic pathways, and functional analysis.";
RL Front. Plant Sci. 2:65-65(2011).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=21690177; DOI=10.1093/pcp/pcr079;
RA Toyokura K., Watanabe K., Oiwaka A., Kusano M., Tameshige T., Tatematsu K.,
RA Matsumoto N., Tsugeki R., Saito K., Okada K.;
RT "Succinic semialdehyde dehydrogenase is involved in the robust patterning
RT of Arabidopsis leaves along the adaxial-abaxial axis.";
RL Plant Cell Physiol. 52:1340-1353(2011).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=25840087; DOI=10.1093/pcp/pcv050;
RA Toyokura K., Yamaguchi K., Shigenobu S., Fukaki H., Tatematsu K., Okada K.;
RT "Mutations in plastidial 5-aminolevulinic acid biosynthesis genes suppress
RT a pleiotropic defect in shoot development of a mitochondrial GABA shunt
RT mutant in Arabidopsis.";
RL Plant Cell Physiol. 56:1229-1238(2015).
CC -!- FUNCTION: Oxidizes specifically succinate semialdehyde. Involved in
CC plant response to environmental stress by preventing the accumulation
CC of reactive oxygen species, probably by regulating proline, gamma-
CC hydroxybutyrate (GHB) and gamma-aminobutyrate (GABA) levels
CC (PubMed:15642352). Required for the maintenance of the shoot apical
CC meristem (SAM) structure and subsequent adaxial-abaxial axis-dependent
CC development of cotyledons and leaves (PubMed:21690177,
CC PubMed:25840087). {ECO:0000269|PubMed:10517851,
CC ECO:0000269|PubMed:12740438, ECO:0000269|PubMed:15642352,
CC ECO:0000269|PubMed:21690177, ECO:0000269|PubMed:25840087}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + succinate semialdehyde = 2 H(+) + NADH +
CC succinate; Xref=Rhea:RHEA:13217, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57706, ChEBI:CHEBI:57945; EC=1.2.1.24;
CC Evidence={ECO:0000269|PubMed:10517851};
CC -!- ACTIVITY REGULATION: Competitive inhibition by NADH. Inhibited by ATP,
CC ADP and AMP. Redox-regulated. Inhibited under oxydizing conditions (By
CC similarity). {ECO:0000250}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=130 uM for NAD(+) (at 24 degrees Celsius)
CC {ECO:0000269|PubMed:10517851};
CC pH dependence:
CC Optimum pH is 9-9.5. {ECO:0000269|PubMed:10517851};
CC -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC {ECO:0000269|PubMed:10517851}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10517851}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:10517851}.
CC -!- TISSUE SPECIFICITY: Expressed in developing leaf tissues.
CC {ECO:0000269|PubMed:21690177}.
CC -!- INDUCTION: Induced during cold (4 degrees Celsius) acclimation
CC (PubMed:17461790). Induced by salt (NaCl) (PubMed:20122158).
CC {ECO:0000269|PubMed:17461790, ECO:0000269|PubMed:20122158}.
CC -!- DISRUPTION PHENOTYPE: Plants are sensitive to UVB and heat stress, and
CC accumulate elevated levels of H(2)O(2) (PubMed:12740438). High light-
CC dependent increased of proline, gamma-hydroxybutyrate (GHB) and gamma-
CC aminobutyrate (GABA) levels. Treatment with gamma-vinyl-gamma-
CC aminobutyrate, a specific gamma-aminobutyrate (GABA)-transaminase
CC inhibitor, prevents the accumulation of reactive oxygen intermediates
CC (ROI) and GHB in ssadh mutants, inhibits cell death, and improves
CC growth (PubMed:15642352). The ssadh mutant defects associated with
CC stress responses are suppressed by POP2 disruption (PubMed:18846220).
CC In enf1, pleiotropic developmental defects including dwarfism, and
CC abnormal leaf shape (including abaxialized and adaxialized leaves) and
CC cotyledon associated with altered GABA and SucA levels in shoots; these
CC phenotypes are partially suppressed by the disruption of POP2/GABAT1,
CC GSA1, GSA2 and HEMA1 (PubMed:21690177, PubMed:25840087). Abnormal FIL
CC expression, especially in the adaxial side, in the leaf primordia
CC (PubMed:21690177). {ECO:0000269|PubMed:12740438,
CC ECO:0000269|PubMed:15642352, ECO:0000269|PubMed:18846220,
CC ECO:0000269|PubMed:21690177, ECO:0000269|PubMed:25840087}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD30232.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF117335; AAF23590.1; -; mRNA.
DR EMBL; AC007202; AAD30232.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36243.1; -; Genomic_DNA.
DR EMBL; AF428367; AAL16297.1; -; mRNA.
DR EMBL; AY056147; AAL07226.1; -; mRNA.
DR PIR; E96825; E96825.
DR RefSeq; NP_178062.1; NM_106592.5.
DR AlphaFoldDB; Q9SAK4; -.
DR SMR; Q9SAK4; -.
DR BioGRID; 29501; 1.
DR STRING; 3702.Q9SAK4; -.
DR MetOSite; Q9SAK4; -.
DR PaxDb; 3702-AT1G79440-1; -.
DR ProteomicsDB; 232490; -.
DR EnsemblPlants; AT1G79440.1; AT1G79440.1; AT1G79440.
DR GeneID; 844282; -.
DR Gramene; AT1G79440.1; AT1G79440.1; AT1G79440.
DR KEGG; ath:AT1G79440; -.
DR Araport; AT1G79440; -.
DR TAIR; AT1G79440; ALDH5F1.
DR eggNOG; KOG2451; Eukaryota.
DR HOGENOM; CLU_005391_5_0_1; -.
DR InParanoid; Q9SAK4; -.
DR OMA; VNGNWID; -.
DR OrthoDB; 3078548at2759; -.
DR PhylomeDB; Q9SAK4; -.
DR BioCyc; ARA:AT1G79440-MONOMER; -.
DR BRENDA; 1.2.1.24; 399.
DR UniPathway; UPA00733; -.
DR PRO; PR:Q9SAK4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SAK4; baseline and differential.
DR Genevisible; Q9SAK4; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0051287; F:NAD binding; IDA:TAIR.
DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IDA:TAIR.
DR GO; GO:0009943; P:adaxial/abaxial axis specification; IMP:UniProtKB.
DR GO; GO:0048825; P:cotyledon development; IMP:UniProtKB.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IDA:TAIR.
DR GO; GO:0006540; P:glutamate decarboxylation to succinate; IDA:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:UniProtKB.
DR GO; GO:0010492; P:maintenance of shoot apical meristem identity; IMP:UniProtKB.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IMP:UniProtKB.
DR GO; GO:1902074; P:response to salt; IEP:UniProtKB.
DR CDD; cd07103; ALDH_F5_SSADH_GabD; 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 InterPro; IPR010102; Succ_semiAld_DH.
DR NCBIfam; TIGR01780; SSADH; 1.
DR PANTHER; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43353:SF5; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 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.
PE 1: Evidence at protein level;
KW Disulfide bond; Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 35..528
FT /note="Succinate-semialdehyde dehydrogenase, mitochondrial"
FT /id="PRO_0000256064"
FT ACT_SITE 297
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 331
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 196..198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P51649"
FT BINDING 222..225
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P51649"
FT BINDING 275..280
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P51649"
FT BINDING 297
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P51649"
FT BINDING 428..430
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT BINDING 488
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P51649"
FT SITE 199
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT DISULFID 331..333
FT /note="In inhibited form"
FT /evidence="ECO:0000250|UniProtKB:P51649"
SQ SEQUENCE 528 AA; 56559 MW; A0DA95A3A592B5B9 CRC64;
MVIGAAARVA IGGCRKLISS HTSLLLVSSQ CRQMSMDAQS VSEKLRSSGL LRTQGLIGGK
WLDSYDNKTI KVNNPATGEI IADVACMGTK ETNDAIASSY EAFTSWSRLT AGERSKVLRR
WYDLLIAHKE ELGQLITLEQ GKPLKEAIGE VAYGASFIEY YAEEAKRVYG DIIPPNLSDR
RLLVLKQPVG VVGAITPWNF PLAMITRKVG PALASGCTVV VKPSELTPLT ALAAAELALQ
AGVPPGALNV VMGNAPEIGD ALLTSPQVRK ITFTGSTAVG KKLMAAAAPT VKKVSLELGG
NAPSIVFDDA DLDVAVKGTL AAKFRNSGQT CVCANRVLVQ DGIYDKFAEA FSEAVQKLEV
GDGFRDGTTQ GPLINDAAVQ KVETFVQDAV SKGAKIIIGG KRHSLGMTFY EPTVIRDVSD
NMIMSKEEIF GPVAPLIRFK TEEDAIRIAN DTIAGLAAYI FTNSVQRSWR VFEALEYGLV
GVNEGLISTE VAPFGGVKQS GLGREGSKYG MDEYLEIKYV CLGDMNRH
//
