Reviewed, UniProtKB/Swiss-Prot Q9SAK4 (SSDH_ARATH)

Names and origin

Protein names

Recommended name:
    Succinate-semialdehyde dehydrogenase, mitochondrial
      Short name=At-SSADH1
    EC=1.2.1.24
Alternative name(s):
    NAD(+)-dependent succinic semialdehyde dehydrogenase
    Aldehyde dehydrogenase family 5 member F1

Gene names

Name:	ALDH5F1
Synonyms:	SSADH1
Ordered Locus Names:	At1g79440
ORF Names:	T8K14.14

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	528 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Oxidizes specifically succinate semialdehyde. Involved in plant response to environmental stress by preventing the accumulation of reactive oxygen species. Ref.1 Ref.4
Catalytic activity	Succinate semialdehyde + NAD+ + H2O = succinate + NADH.
Enzyme regulation	Competitive inhibition by NADH. Inhibited by ATP, ADP and AMP. Ref.1
Pathway	Amino-acid degradation; 4-aminobutanoate degradation.
Subunit structure	Homotetramer. Ref.1
Subcellular location	Mitochondrion matrix. Ref.1
Disruption phenotype	Plants are sensitive to UVB and heat stress, and accumulate elevated levels of H2O2. Ref.4
Sequence similarities	Belongs to the aldehyde dehydrogenase family.
biophysicochemical properties	Kinetic parameters: KM=130 µM for NAD+ (at 24 degrees Celsius) pH dependence: Optimum pH is 9-9.5.
Sequence caution	The sequence AAD30232.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	gamma-aminobutyric acid catabolic process Ref.1 Inferred from direct assay. Source: TAIR glutamate decarboxylation to succinate Ref.1 Inferred from direct assay. Source: TAIR oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxygen and reactive oxygen species metabolic process Inferred from mutant phenotype. Source: TAIR response to heat Ref.4 Inferred from mutant phenotype. Source: TAIR response to light stimulus Ref.4 Inferred from mutant phenotype. Source: TAIR
Cellular component	chloroplast Inferred from direct assay. Source: TAIR mitochondrial matrix Ref.1 Inferred from direct assay. Source: TAIR
Molecular function	NAD or NADH binding Inferred from direct assay. Source: TAIR succinate-semialdehyde dehydrogenase activity Ref.1 Inferred from direct assay. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 24	24	Mitochondrion Potential
	Chain	25 – 528	504	Succinate-semialdehyde dehydrogenase, mitochondrial		PRO_0000256064
Regions
	Nucleotide binding	275 – 280	6	NAD By similarity
Sites
	Active site	297	1	Proton acceptor By similarity
	Active site	331	1	Nucleophile By similarity
	Site	199	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9SAK4-1 [UniParc]. Last modified October 31, 2006. Version 2. Checksum: A0DA95A3A592B5B9	FASTA	528	56,559
	10 20 30 40 50 60 MVIGAAARVA IGGCRKLISS HTSLLLVSSQ CRQMSMDAQS VSEKLRSSGL LRTQGLIGGK 70 80 90 100 110 120 WLDSYDNKTI KVNNPATGEI IADVACMGTK ETNDAIASSY EAFTSWSRLT AGERSKVLRR 130 140 150 160 170 180 WYDLLIAHKE ELGQLITLEQ GKPLKEAIGE VAYGASFIEY YAEEAKRVYG DIIPPNLSDR 190 200 210 220 230 240 RLLVLKQPVG VVGAITPWNF PLAMITRKVG PALASGCTVV VKPSELTPLT ALAAAELALQ 250 260 270 280 290 300 AGVPPGALNV VMGNAPEIGD ALLTSPQVRK ITFTGSTAVG KKLMAAAAPT VKKVSLELGG 310 320 330 340 350 360 NAPSIVFDDA DLDVAVKGTL AAKFRNSGQT CVCANRVLVQ DGIYDKFAEA FSEAVQKLEV 370 380 390 400 410 420 GDGFRDGTTQ GPLINDAAVQ KVETFVQDAV SKGAKIIIGG KRHSLGMTFY EPTVIRDVSD 430 440 450 460 470 480 NMIMSKEEIF GPVAPLIRFK TEEDAIRIAN DTIAGLAAYI FTNSVQRSWR VFEALEYGLV 490 500 510 520 GVNEGLISTE VAPFGGVKQS GLGREGSKYG MDEYLEIKYV CLGDMNRH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Plant succinic semialdehyde dehydrogenase. Cloning, purification, localization in mitochondria, and regulation by adenine nucleotides." Busch K.B., Fromm H. Plant Physiol. 121:589-597(1999) [PubMed: 10517851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Mitochondrial succinic-semialdehyde dehydrogenase of the gamma-aminobutyrate shunt is required to restrict levels of reactive oxygen intermediates in plants." Bouche N., Fait A., Bouchez D., Moeller S.G., Fromm H. Proc. Natl. Acad. Sci. U.S.A. 100:6843-6848(2003) [PubMed: 12740438] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]	"The ALDH gene superfamily of Arabidopsis." Kirch H.-H., Bartels D., Wei Y., Schnable P.S., Wood A.J. Trends Plant Sci. 9:371-377(2004) [PubMed: 15358267] [Abstract] Cited for: NOMENCLATURE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF117335 mRNA. Translation: AAF23590.1. AC007202 Genomic DNA. Translation: AAD30232.1. Sequence problems. AF428367 mRNA. Translation: AAL16297.1. AY056147 mRNA. Translation: AAL07226.1.
IPI	IPI00532908.
PIR	E96825.
RefSeq	NP_178062.1.
UniGene	At.11884
3D structure databases
HSSP	HSSP built from PDB template 1BXS based on UniProtKB P51977.
ModBase	Search...
Proteomic databases
PRIDE	Q9SAK4.
Genome annotation databases
GeneID	844282.
GenomeReviews	Gene locus AT1G79440 in contig CT485782_GR.
KEGG	ath:AT1G79440.
NMPDR	fig|3702.1.peg.7506.
Organism-specific databases
GeneFarm	4340.
TAIR	At1g79440.
Phylogenomic databases
OMA	Q9SAK4. PTQRADA.
Enzyme and pathway databases
BRENDA	1.2.1.24. 302.
Family and domain databases
InterPro	IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH. IPR010102. Succ_semiAld_DH. [Graphical view]
Gene3D	G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHER	PTHR11699. Aldehyde_dehyd. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
TIGRFAMs	TIGR01780. SSADH. 1 hit.
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SSDH_ARATH

Accession

Primary (citable) accession number: Q9SAK4
Secondary accession number(s): Q9SEK4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 31, 2006
Last modified:	June 16, 2009
This is version 56 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)