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P76149

- SAD_ECOLI

UniProt

P76149 - SAD_ECOLI

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Protein

Succinate semialdehyde dehydrogenase [NAD(P)+] Sad

Gene

sad

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

Pathwayi

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

  1. succinate-semialdehyde dehydrogenase (NAD+) activity Source: UniProtKB
  2. succinate-semialdehyde dehydrogenase [NAD(P)+] activity Source: EcoCyc

GO - Biological processi

  1. arginine catabolic process Source: EcoCyc
  2. gamma-aminobutyric acid catabolic process Source: EcoliWiki
  3. nitrogen compound metabolic process Source: UniProtKB
  4. 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: Chromosome, UP000000625: 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

Gene expression databases

GenevestigatoriP76149.

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.
OMAiSHIIENQ.
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.
YP_489788.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74598; AAC74598; b1525.
BAA15208; BAA15208; BAA15208.
GeneIDi12932699.
947440.
KEGGiecj:Y75_p1500.
eco: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 .
PIRi H64906.
RefSeqi NP_416042.2. NC_000913.3.
YP_489788.1. NC_007779.1.

3D structure databases

ProteinModelPortali P76149.
SMRi P76149. Positions 6-462.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-12758N.
IntActi P76149. 1 interaction.
STRINGi 511145.b1525.

2D gel databases

SWISS-2DPAGE P76149.

Proteomic databases

PaxDbi P76149.
PRIDEi P76149.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74598 ; AAC74598 ; b1525 .
BAA15208 ; BAA15208 ; BAA15208 .
GeneIDi 12932699.
947440.
KEGGi ecj:Y75_p1500.
eco:b1525.
PATRICi 32118348. VBIEscCol129921_1594.

Organism-specific databases

EchoBASEi EB3578.
EcoGenei EG13817. yneI.

Phylogenomic databases

eggNOGi COG1012.
HOGENOMi HOG000271513.
InParanoidi P76149.
KOi K08324.
OMAi SHIIENQ.
OrthoDBi EOG6BS8QW.
PhylomeDBi P76149.

Enzyme and pathway databases

UniPathwayi UPA00733 .
BioCyci EcoCyc:G6811-MONOMER.
ECOL316407:JW5247-MONOMER.
MetaCyc:G6811-MONOMER.

Miscellaneous databases

PROi P76149.

Gene expression databases

Genevestigatori P76149.

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.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view ]
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
SUPFAMi SSF53720. SSF53720. 1 hit.
PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 115 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