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P51650

- SSDH_RAT

UniProt

P51650 - SSDH_RAT

Protein

Succinate-semialdehyde dehydrogenase, mitochondrial

Gene

Aldh5a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (08 Apr 2008)
      Previous versions | rss
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    Functioni

    Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA).By similarity

    Catalytic activityi

    Succinate semialdehyde + NAD+ + H2O = succinate + NADH.

    Enzyme regulationi

    Redox-regulated. Inhibited under oxydizing conditions By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei193 – 1931Transition state stabilizerBy similarity
    Binding sitei201 – 2011NADBy similarity
    Binding sitei201 – 2011SubstrateBy similarity
    Active sitei294 – 2941Proton acceptorPROSITE-ProRule annotation
    Binding sitei322 – 3221SubstrateBy similarity
    Active sitei328 – 3281NucleophilePROSITE-ProRule annotation
    Binding sitei486 – 4861SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi216 – 2194NADBy similarity
    Nucleotide bindingi272 – 2776NADBy similarity

    GO - Molecular functioni

    1. carboxylic acid binding Source: RGD
    2. NAD binding Source: RGD
    3. succinate-semialdehyde dehydrogenase (NAD+) activity Source: UniProtKB
    4. succinate-semialdehyde dehydrogenase [NAD(P)+] activity Source: InterPro

    GO - Biological processi

    1. central nervous system development Source: UniProtKB
    2. gamma-aminobutyric acid catabolic process Source: UniProtKB
    3. oxidation-reduction process Source: UniProtKB
    4. succinate metabolic process Source: RGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    SABIO-RKP51650.
    UniPathwayiUPA00733.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Succinate-semialdehyde dehydrogenase, mitochondrial (EC:1.2.1.24)
    Alternative name(s):
    Aldehyde dehydrogenase family 5 member A1
    NAD(+)-dependent succinic semialdehyde dehydrogenase
    Gene namesi
    Name:Aldh5a1
    Synonyms:Ssadh
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi621422. Aldh5a1.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3535Mitochondrion2 PublicationsAdd
    BLAST
    Chaini36 – 523488Succinate-semialdehyde dehydrogenase, mitochondrialPRO_0000056567Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei114 – 1141N6-acetyllysine; alternateBy similarity
    Modified residuei114 – 1141N6-succinyllysine; alternateBy similarity
    Modified residuei123 – 1231N6-succinyllysineBy similarity
    Modified residuei172 – 1721N6-succinyllysineBy similarity
    Modified residuei253 – 2531N6-acetyllysine; alternateBy similarity
    Modified residuei253 – 2531N6-succinyllysine; alternateBy similarity
    Disulfide bondi328 ↔ 330In inhibited formBy similarity
    Modified residuei353 – 3531N6-acetyllysineBy similarity
    Modified residuei390 – 3901N6-succinyllysineBy similarity
    Modified residuei399 – 3991N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    PaxDbiP51650.
    PRIDEiP51650.

    2D gel databases

    World-2DPAGE0004:P51650.

    PTM databases

    PhosphoSiteiP51650.

    Expressioni

    Tissue specificityi

    Brain, pancreas, heart, liver, skeletal muscle, kidney. Lower in spleen, lung, kidney and testis.

    Gene expression databases

    GenevestigatoriP51650.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000035601.

    Structurei

    3D structure databases

    ProteinModelPortaliP51650.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1012.
    HOGENOMiHOG000271509.
    HOVERGENiHBG108515.
    InParanoidiP51650.
    PhylomeDBiP51650.

    Family and domain databases

    Gene3Di3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    InterProiIPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016160. Ald_DH_CS_CYS.
    IPR029510. Ald_DH_CS_GLU.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR010102. Succ_semiAld_DH.
    [Graphical view]
    PfamiPF00171. Aldedh. 1 hit.
    [Graphical view]
    SUPFAMiSSF53720. SSF53720. 1 hit.
    TIGRFAMsiTIGR01780. SSADH. 1 hit.
    PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P51650-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MATCFLLRNF CAARPALRPP GRLLREPAGA QRRSYVGGPA DLHADLLRGD    50
    SFVGGRWLPT PATFPVYDPA SGAKLGTVAD CGVPEARAAV RAAYDAFSSW 100
    KEISVKERSS LLRKWYDLMI QNKDELAKII TAESGKPLKE AQGEILYSAF 150
    FLEWFSEEAR RVYGDIIYTS AKDKRGLVLK QPVGVASIIT PWNFPSAMIT 200
    RKVGAALAAG CTVVVKPAED TPYSALALAQ LANQAGIPPG VYNVIPCSRT 250
    KAKEVGEVLC TDPLVSKISF TGSTATGKIL LHHAANSVKR VSMELGGLAP 300
    FIVFDSANVD QAVAGAMASK FRNAGQTCVC SNRFLVQRGI HDSFVTKFAE 350
    AMKKSLRVGN GFEEGTTQGP LINEKAVEKV EKHVNDAVAK GATVVTGGKR 400
    HQSGGNFFEP TLLSNVTRDM LCITEETFGP VAPVIKFDKE EEAVAIANAA 450
    DVGLAGYFYS QDPAQIWRVA EQLEVGMVGV NEGLISSVEC PFGGVKQSGL 500
    GREGSKYGID EYLEVKYVCY GGL 523
    Length:523
    Mass (Da):56,131
    Last modified:April 8, 2008 - v2
    Checksum:i4CA521139C9FA98F
    GO
    Isoform Short (identifier: P51650-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         107-134: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:495
    Mass (Da):52,798
    Checksum:iFC69A1D9215CEF5F
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei107 – 13428Missing in isoform Short. 1 PublicationVSP_001284Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03105019 Genomic DNA. No translation available.
    L34821 mRNA. Translation: AAA67058.1.
    PIRiI61704.
    UniGeneiRn.10070.

    Genome annotation databases

    UCSCiRGD:621422. rat. [P51650-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03105019 Genomic DNA. No translation available.
    L34821 mRNA. Translation: AAA67058.1 .
    PIRi I61704.
    UniGenei Rn.10070.

    3D structure databases

    ProteinModelPortali P51650.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000035601.

    PTM databases

    PhosphoSitei P51650.

    2D gel databases

    World-2DPAGE 0004:P51650.

    Proteomic databases

    PaxDbi P51650.
    PRIDEi P51650.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:621422. rat. [P51650-1 ]

    Organism-specific databases

    RGDi 621422. Aldh5a1.

    Phylogenomic databases

    eggNOGi COG1012.
    HOGENOMi HOG000271509.
    HOVERGENi HBG108515.
    InParanoidi P51650.
    PhylomeDBi P51650.

    Enzyme and pathway databases

    UniPathwayi UPA00733 .
    SABIO-RK P51650.

    Miscellaneous databases

    PROi P51650.

    Gene expression databases

    Genevestigatori P51650.

    Family and domain databases

    Gene3Di 3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    InterProi IPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016160. Ald_DH_CS_CYS.
    IPR029510. Ald_DH_CS_GLU.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR010102. Succ_semiAld_DH.
    [Graphical view ]
    Pfami PF00171. Aldedh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53720. SSF53720. 1 hit.
    TIGRFAMsi TIGR01780. SSADH. 1 hit.
    PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    2. "Molecular cloning of the mature NAD(+)-dependent succinic semialdehyde dehydrogenase from rat and human. cDNA isolation, evolutionary homology, and tissue expression."
      Chambliss K.L., Caudle D.L., Hinson D.D., Moomaw C.R., Slaughter C.A., Jakobs C., Gibson K.M.
      J. Biol. Chem. 270:461-467(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), PROTEIN SEQUENCE OF 36-84; 92-101; 129-153; 162-172; 303-311; 419-425 AND 503-526.
      Strain: Sprague-Dawley.
      Tissue: Brain.
    3. Lubec G., Afjehi-Sadat L.
      Submitted (NOV-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 36-48; 161-172 AND 401-418, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Spinal cord.

    Entry informationi

    Entry nameiSSDH_RAT
    AccessioniPrimary (citable) accession number: P51650
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 110 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3