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UniProtKB/Swiss-Prot entry Q9SAK4


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SSDH_ARATH
Primary accession number Q9SAK4
Secondary accession number Q9SEK4
Integrated into Swiss-Prot on October 31, 2006
Sequence was last modified on October 31, 2006 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 48)
Name and origin of the protein
Protein name Succinate-semialdehyde dehydrogenase, mitochondrial [Precursor]
Synonyms At-SSADH1
EC 1.2.1.24
NAD(+)-dependent succinic semialdehyde dehydrogenase
Aldehyde dehydrogenase family 5 member F1
Gene name
Name: ALDH5F1
Synonyms: SSADH1
OrderedLocusNames: At1g79440
ORFNames: T8K14.14
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
DOI=10.1104/pp.121.2.589; PubMed=10517851 [NCBI, ExPASy, EBI, Israel, Japan]
Busch K.B., Fromm H.;
"Plant succinic semialdehyde dehydrogenase. Cloning, purification, localization in mitochondria, and regulation by adenine nucleotides.";
Plant Physiol. 121:589-597(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
FUNCTION.
DOI=10.1073/pnas.1037532100; PubMed=12740438 [NCBI, ExPASy, EBI, Israel, Japan]
Bouche N., Fait A., Bouchez D., Moeller S.G., Fromm H.;
"Mitochondrial succinic-semialdehyde dehydrogenase of the gamma-aminobutyrate shunt is required to restrict levels of reactive oxygen intermediates in plants.";
Proc. Natl. Acad. Sci. U.S.A. 100:6843-6848(2003).
[5]
NOMENCLATURE.
DOI=10.1016/j.tplants.2004.06.004; PubMed=15358267 [NCBI, ExPASy, EBI, Israel, Japan]
Kirch H.-H., Bartels D., Wei Y., Schnable P.S., Wood A.J.;
"The ALDH gene superfamily of Arabidopsis.";
Trends Plant Sci. 9:371-377(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF117335; AAF23590.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC007202; AAD30232.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF428367; AAL16297.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY056147; AAL07226.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E96825; E96825.
RefSeq NP_178062.1; -.
UniGene At.11884
3D structure databases
HSSP P51977; 1BXS. [HSSP ENTRY / PDB]
ModBase Q9SAK4.
Organism-specific databases
GeneFarm 4340; -.
TAIR At1g79440; -.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004777; Molecular function: succinate-semialdehyde dehydrogenase activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
IPR010102; Succ_semiAld_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01780; SSADH; 1.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
BLOCKS Q9SAK4.
Genome annotation databases
GeneID 844282; -.
GenomeReviews CT485782_GR; AT1G79440.
KEGG ath:AT1G79440; -.
NMPDR fig|3702.1.peg.7506; -.
Other
ProtoNet Q9SAK4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Mitochondrion; NAD; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    24  24     Mitochondrion (Potential). 
CHAIN   25   528  504     Succinate-semialdehyde dehydrogenase, mitochondrial. PRO_0000256064
NP_BIND   275   280  6     NAD (By similarity). 
ACT_SITE   297   297        Proton acceptor (By similarity). 
ACT_SITE   331   331        Nucleophile (By similarity). 
SITE   199   199  1     Transition state stabilizer (By similarity). 
Sequence information
Length: 528 AA [This is the length of the unprocessed precursor] Molecular weight: 56559 Da [This is the MW of the unprocessed precursor] CRC64: A0DA95A3A592B5B9 [This is a checksum on the sequence]
        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 

Q9SAK4 in FASTA format

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