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Protein

Succinate semialdehyde dehydrogenase [NAD(P)+] Sad

Gene

sad

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NAD+-dependent oxidation of succinate semialdehyde to succinate. It acts preferentially with NAD as cosubstrate but can also use NADP. Prevents the toxic accumulation of succinate semialdehyde (SSA) and plays an important role when arginine and putrescine are used as the sole nitrogen or carbon sources.4 Publications

Catalytic activityi

Succinate semialdehyde + NAD(P)+ + H2O = succinate + NAD(P)H.1 Publication

Kineticsi

The enzyme reduced NADP at 15 % of the rate of NAD reduction.

  1. KM=13.3 µM for succinate semialdehyde (with 0.6 mM NAD, at pH 8 and at 30 degrees Celsius)1 Publication
  2. KM=33.7 µM for succinate semialdehyde (with 0.1 mM NAD, at pH 8 and at 30 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 8.2. Activity decreases sharply as the pH is raised above pH 9.2.1 Publication

    Pathway:i4-aminobutanoate degradation

    This protein is involved in the pathway 4-aminobutanoate degradation, which is part of Amino-acid degradation.
    View all proteins of this organism that are known to be involved in the pathway 4-aminobutanoate degradation and in Amino-acid degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei234 – 2341Proton acceptorPROSITE-ProRule annotation
    Binding sitei235 – 2351NAD or NADP; via carbonyl oxygenBy similarity
    Active sitei268 – 2681NucleophilePROSITE-ProRule annotation
    Binding sitei365 – 3651NAD or NADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi136 – 1372NAD or NADPBy similarity
    Nucleotide bindingi160 – 1634NAD or NADPBy similarity
    Nucleotide bindingi212 – 2176NAD or NADPBy similarity

    GO - Molecular functioni

    GO - Biological processi

    • arginine catabolic process Source: EcoCyc
    • gamma-aminobutyric acid catabolic process Source: EcoliWiki
    • nitrogen compound metabolic process Source: UniProtKB
    • putrescine catabolic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:G6811-MONOMER.
    ECOL316407:JW5247-MONOMER.
    MetaCyc:G6811-MONOMER.
    UniPathwayiUPA00733.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Succinate semialdehyde dehydrogenase [NAD(P)+] Sad (EC:1.2.1.16)
    Short name:
    SSADH
    Short name:
    SSDH
    Gene namesi
    Name:sad
    Synonyms:yneI
    Ordered Locus Names:b1525, JW5247
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13817. yneI.

    Pathology & Biotechi

    Disruption phenotypei

    Cells are unable to grow on 4-hydroxyphenylacetate.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 462462Succinate semialdehyde dehydrogenase [NAD(P)+] SadPRO_0000056598Add
    BLAST

    Proteomic databases

    PaxDbiP76149.
    PRIDEiP76149.

    2D gel databases

    SWISS-2DPAGEP76149.

    Expressioni

    Inductioni

    By p-hydroxyphenylacetate, succinate semialdehyde (SSA) and putrescine. Highly expressed under several stress conditions together with many genes related to the metabolism of nitrogen compounds.2 Publications

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    DIPiDIP-12758N.
    IntActiP76149. 1 interaction.
    STRINGi511145.b1525.

    Structurei

    3D structure databases

    ProteinModelPortaliP76149.
    SMRiP76149. Positions 6-462.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG1012.
    HOGENOMiHOG000271513.
    InParanoidiP76149.
    KOiK08324.
    OMAiDHNATET.
    OrthoDBiEOG6BS8QW.
    PhylomeDBiP76149.

    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.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    [Graphical view]
    PfamiPF00171. Aldedh. 1 hit.
    [Graphical view]
    SUPFAMiSSF53720. SSF53720. 1 hit.
    PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P76149-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTITPATHAI SINPATGEQL SVLPWAGADD IENALQLAAA GFRDWRETNI
    60 70 80 90 100
    DYRAEKLRDI GKALRARSEE MAQMITREMG KPINQARAEV AKSANLCDWY
    110 120 130 140 150
    AEHGPAMLKA EPTLVENQQA VIEYRPLGTI LAIMPWNFPL WQVMRGAVPI
    160 170 180 190 200
    ILAGNGYLLK HAPNVMGCAQ LIAQVFKDAG IPQGVYGWLN ADNDGVSQMI
    210 220 230 240 250
    KDSRIAAVTV TGSVRAGAAI GAQAGAALKK CVLELGGSDP FIVLNDADLE
    260 270 280 290 300
    LAVKAAVAGR YQNTGQVCAA AKRFIIEEGI ASAFTERFVA AAAALKMGDP
    310 320 330 340 350
    RDEENALGPM ARFDLRDELH HQVEKTLAQG ARLLLGGEKM AGAGNYYPPT
    360 370 380 390 400
    VLANVTPEMT AFREEMFGPV AAITIAKDAE HALELANDSE FGLSATIFTT
    410 420 430 440 450
    DETQARQMAA RLECGGVFIN GYCASDARVA FGGVKKSGFG RELSHFGLHE
    460
    FCNIQTVWKD RI
    Length:462
    Mass (Da):49,718
    Last modified:December 15, 1998 - v2
    Checksum:i78BEF85ED538C684
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC74598.2.
    AP009048 Genomic DNA. Translation: BAA15208.2.
    PIRiH64906.
    RefSeqiNP_416042.2. NC_000913.3.
    WP_000156615.1. NZ_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74598; AAC74598; b1525.
    BAA15208; BAA15208; BAA15208.
    GeneIDi947440.
    KEGGieco:b1525.
    PATRICi32118348. VBIEscCol129921_1594.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC74598.2.
    AP009048 Genomic DNA. Translation: BAA15208.2.
    PIRiH64906.
    RefSeqiNP_416042.2. NC_000913.3.
    WP_000156615.1. NZ_CP010445.1.

    3D structure databases

    ProteinModelPortaliP76149.
    SMRiP76149. Positions 6-462.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-12758N.
    IntActiP76149. 1 interaction.
    STRINGi511145.b1525.

    2D gel databases

    SWISS-2DPAGEP76149.

    Proteomic databases

    PaxDbiP76149.
    PRIDEiP76149.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74598; AAC74598; b1525.
    BAA15208; BAA15208; BAA15208.
    GeneIDi947440.
    KEGGieco:b1525.
    PATRICi32118348. VBIEscCol129921_1594.

    Organism-specific databases

    EchoBASEiEB3578.
    EcoGeneiEG13817. yneI.

    Phylogenomic databases

    eggNOGiCOG1012.
    HOGENOMiHOG000271513.
    InParanoidiP76149.
    KOiK08324.
    OMAiDHNATET.
    OrthoDBiEOG6BS8QW.
    PhylomeDBiP76149.

    Enzyme and pathway databases

    UniPathwayiUPA00733.
    BioCyciEcoCyc:G6811-MONOMER.
    ECOL316407:JW5247-MONOMER.
    MetaCyc:G6811-MONOMER.

    Miscellaneous databases

    PROiP76149.

    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.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    [Graphical view]
    PfamiPF00171. Aldedh. 1 hit.
    [Graphical view]
    SUPFAMiSSF53720. SSF53720. 1 hit.
    PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Succinic semialdehyde dehydrogenases of Escherichia coli: their role in the degradation of p-hydroxyphenylacetate and gamma-aminobutyrate."
      Donnelly M.I., Cooper R.A.
      Eur. J. Biochem. 113:555-561(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A NAD(P)-DEPENDENT SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: K12.
    5. "Two succinic semialdehyde dehydrogenases are induced when Escherichia coli K-12 Is grown on gamma-aminobutyrate."
      Donnelly M.I., Cooper R.A.
      J. Bacteriol. 145:1425-1427(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A NAD(P)-DEPENDENT SUCCINATE-SEMIALDEHYDE DEHYDROGENASE.
      Strain: K12.
    6. "An Escherichia coli mutant defective in the NAD-dependent succinate semialdehyde dehydrogenase."
      Skinner M.A., Cooper R.A.
      Arch. Microbiol. 132:270-275(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
      Strain: K12.
    7. "Computational prediction and experimental verification of the gene encoding the NAD+/NADP+-dependent succinate semialdehyde dehydrogenase in Escherichia coli."
      Fuhrer T., Chen L., Sauer U., Vitkup D.
      J. Bacteriol. 189:8073-8078(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE METABOLISM OF NITROGEN COMPOUNDS AND AS A NAD(P)-DEPENDENT SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, INDUCTION.
      Strain: K12.
    8. "A putrescine-inducible pathway comprising PuuE-YneI in which gamma-aminobutyrate is degraded into succinate in Escherichia coli K-12."
      Kurihara S., Kato K., Asada K., Kumagai H., Suzuki H.
      J. Bacteriol. 192:4582-4591(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE METABOLISM OF CARBON COMPOUNDS, INDUCTION.
      Strain: K12.

    Entry informationi

    Entry nameiSAD_ECOLI
    AccessioniPrimary (citable) accession number: P76149
    Secondary accession number(s): P78220, P78286
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: December 15, 1998
    Last modified: July 22, 2015
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.