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P76149 (SAD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Succinate semialdehyde dehydrogenase [NAD(P)+] Sad
Short name=SSADH
Short name=SSDH
EC=1.2.1.16
Gene names
Name:sad
Synonyms:yneI
Ordered Locus Names:b1525, JW5247
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5 Ref.7 Ref.8

Catalytic activity

Succinate semialdehyde + NAD(P)+ + H2O = succinate + NAD(P)H. Ref.7

Pathway

Amino-acid degradation; 4-aminobutanoate degradation.

Subunit structure

Homodimer. Ref.4

Induction

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. Ref.7 Ref.8

Disruption phenotype

Cells are unable to grow on 4-hydroxyphenylacetate. Ref.6

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

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

KM=13.3 µM for succinate semialdehyde (with 0.6 mM NAD, at pH 8 and at 30 degrees Celsius) Ref.4

KM=33.7 µM for succinate semialdehyde (with 0.1 mM NAD, at pH 8 and at 30 degrees Celsius)

pH dependence:

Optimum pH is 8.2. Activity decreases sharply as the pH is raised above pH 9.2.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462Succinate semialdehyde dehydrogenase [NAD(P)+] Sad
PRO_0000056598

Regions

Nucleotide binding136 – 1372NAD or NADP By similarity
Nucleotide binding160 – 1634NAD or NADP By similarity
Nucleotide binding212 – 2176NAD or NADP By similarity

Sites

Active site2341Proton acceptor By similarity
Active site2681Nucleophile By similarity
Binding site2351NAD or NADP; via carbonyl oxygen By similarity
Binding site3651NAD or NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
P76149 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 78BEF85ED538C684

FASTA46249,718
        10         20         30         40         50         60 
MTITPATHAI SINPATGEQL SVLPWAGADD IENALQLAAA GFRDWRETNI DYRAEKLRDI 

        70         80         90        100        110        120 
GKALRARSEE MAQMITREMG KPINQARAEV AKSANLCDWY AEHGPAMLKA EPTLVENQQA 

       130        140        150        160        170        180 
VIEYRPLGTI LAIMPWNFPL WQVMRGAVPI ILAGNGYLLK HAPNVMGCAQ LIAQVFKDAG 

       190        200        210        220        230        240 
IPQGVYGWLN ADNDGVSQMI KDSRIAAVTV TGSVRAGAAI GAQAGAALKK CVLELGGSDP 

       250        260        270        280        290        300 
FIVLNDADLE LAVKAAVAGR YQNTGQVCAA AKRFIIEEGI ASAFTERFVA AAAALKMGDP 

       310        320        330        340        350        360 
RDEENALGPM ARFDLRDELH HQVEKTLAQG ARLLLGGEKM AGAGNYYPPT VLANVTPEMT 

       370        380        390        400        410        420 
AFREEMFGPV AAITIAKDAE HALELANDSE FGLSATIFTT DETQARQMAA RLECGGVFIN 

       430        440        450        460 
GYCASDARVA FGGVKKSGFG RELSHFGLHE FCNIQTVWKD RI

« Hide

References

« Hide 'large scale' references
[1]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U00096 Genomic DNA. Translation: AAC74598.2.
AP009048 Genomic DNA. Translation: BAA15208.2.
PIRH64906.
RefSeqNP_416042.2. NC_000913.2.
YP_489788.1. NC_007779.1.

3D structure databases

ProteinModelPortalP76149.
SMRP76149. Positions 6-462.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-12758N.
IntActP76149. 1 interaction.
STRING511145.b1525.

2D gel databases

SWISS-2DPAGEP76149.

Proteomic databases

PaxDbP76149.
PRIDEP76149.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74598; AAC74598; b1525.
BAA15208; BAA15208; BAA15208.
GeneID12932699.
947440.
KEGGecj:Y75_p1500.
eco:b1525.
PATRIC32118348. VBIEscCol129921_1594.

Organism-specific databases

EchoBASEEB3578.
EcoGeneEG13817. yneI.

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271513.
KOK08324.
OMATVWKDRV.
ProtClustDBPRK13968.

Enzyme and pathway databases

BioCycEcoCyc:G6811-MONOMER.
ECOL316407:JW5247-MONOMER.
MetaCyc:G6811-MONOMER.
UniPathwayUPA00733.

Gene expression databases

GenevestigatorP76149.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSAD_ECOLI
AccessionPrimary (citable) accession number: P76149
Secondary accession number(s): P78220, P78286
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: May 1, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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