ID SAD_ECOLI Reviewed; 462 AA.
AC P76149; P78220; P78286;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 27-MAR-2024, entry version 162.
DE RecName: Full=Succinate semialdehyde dehydrogenase [NAD(P)+] Sad;
DE Short=SSADH;
DE Short=SSDH;
DE EC=1.2.1.16;
GN Name=sad; Synonyms=yneI; OrderedLocusNames=b1525, JW5247;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION AS A NAD(P)-DEPENDENT SUCCINATE-SEMIALDEHYDE DEHYDROGENASE,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=7011797; DOI=10.1111/j.1432-1033.1981.tb05098.x;
RA Donnelly M.I., Cooper R.A.;
RT "Succinic semialdehyde dehydrogenases of Escherichia coli: their role in
RT the degradation of p-hydroxyphenylacetate and gamma-aminobutyrate.";
RL Eur. J. Biochem. 113:555-561(1981).
RN [5]
RP FUNCTION AS A NAD(P)-DEPENDENT SUCCINATE-SEMIALDEHYDE DEHYDROGENASE.
RC STRAIN=K12;
RX PubMed=7009588; DOI=10.1128/jb.145.3.1425-1427.1981;
RA Donnelly M.I., Cooper R.A.;
RT "Two succinic semialdehyde dehydrogenases are induced when Escherichia coli
RT K-12 Is grown on gamma-aminobutyrate.";
RL J. Bacteriol. 145:1425-1427(1981).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=6756331; DOI=10.1007/bf00407964;
RA Skinner M.A., Cooper R.A.;
RT "An Escherichia coli mutant defective in the NAD-dependent succinate
RT semialdehyde dehydrogenase.";
RL Arch. Microbiol. 132:270-275(1982).
RN [7]
RP FUNCTION IN THE METABOLISM OF NITROGEN COMPOUNDS AND AS A NAD(P)-DEPENDENT
RP SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=17873044; DOI=10.1128/jb.01027-07;
RA Fuhrer T., Chen L., Sauer U., Vitkup D.;
RT "Computational prediction and experimental verification of the gene
RT encoding the NAD+/NADP+-dependent succinate semialdehyde dehydrogenase in
RT Escherichia coli.";
RL J. Bacteriol. 189:8073-8078(2007).
RN [8]
RP FUNCTION IN THE METABOLISM OF CARBON COMPOUNDS, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=20639325; DOI=10.1128/jb.00308-10;
RA Kurihara S., Kato K., Asada K., Kumagai H., Suzuki H.;
RT "A putrescine-inducible pathway comprising PuuE-YneI in which gamma-
RT aminobutyrate is degraded into succinate in Escherichia coli K-12.";
RL J. Bacteriol. 192:4582-4591(2010).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of succinate
CC semialdehyde to succinate. It acts preferentially with NAD as
CC cosubstrate but can also use NADP. Prevents the toxic accumulation of
CC succinate semialdehyde (SSA) and plays an important role when arginine
CC and putrescine are used as the sole nitrogen or carbon sources.
CC {ECO:0000269|PubMed:17873044, ECO:0000269|PubMed:20639325,
CC ECO:0000269|PubMed:7009588, ECO:0000269|PubMed:7011797}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + succinate semialdehyde = 2 H(+) + NADH +
CC succinate; Xref=Rhea:RHEA:13217, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57706, ChEBI:CHEBI:57945; EC=1.2.1.16;
CC Evidence={ECO:0000269|PubMed:17873044};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) + succinate semialdehyde = 2 H(+) + NADPH +
CC succinate; Xref=Rhea:RHEA:13213, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57706,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.16;
CC Evidence={ECO:0000269|PubMed:17873044};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.3 uM for succinate semialdehyde (with 0.6 mM NAD, at pH 8 and
CC at 30 degrees Celsius) {ECO:0000269|PubMed:7011797};
CC KM=33.7 uM for succinate semialdehyde (with 0.1 mM NAD, at pH 8 and
CC at 30 degrees Celsius) {ECO:0000269|PubMed:7011797};
CC Note=The enzyme reduced NADP at 15 % of the rate of NAD reduction.;
CC pH dependence:
CC Optimum pH is 8.2. Activity decreases sharply as the pH is raised
CC above pH 9.2. {ECO:0000269|PubMed:7011797};
CC -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7011797}.
CC -!- INDUCTION: By p-hydroxyphenylacetate, succinate semialdehyde (SSA) and
CC putrescine. Highly expressed under several stress conditions together
CC with many genes related to the metabolism of nitrogen compounds.
CC {ECO:0000269|PubMed:17873044, ECO:0000269|PubMed:20639325}.
CC -!- DISRUPTION PHENOTYPE: Cells are unable to grow on 4-
CC hydroxyphenylacetate. {ECO:0000269|PubMed:6756331}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC74598.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15208.2; -; Genomic_DNA.
DR PIR; H64906; H64906.
DR RefSeq; NP_416042.2; NC_000913.3.
DR RefSeq; WP_000156615.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P76149; -.
DR SMR; P76149; -.
DR BioGRID; 4261693; 15.
DR DIP; DIP-12758N; -.
DR IntAct; P76149; 1.
DR STRING; 511145.b1525; -.
DR SWISS-2DPAGE; P76149; -.
DR jPOST; P76149; -.
DR PaxDb; 511145-b1525; -.
DR EnsemblBacteria; AAC74598; AAC74598; b1525.
DR GeneID; 947440; -.
DR KEGG; ecj:JW5247; -.
DR KEGG; eco:b1525; -.
DR PATRIC; fig|1411691.4.peg.741; -.
DR EchoBASE; EB3578; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_0_6; -.
DR InParanoid; P76149; -.
DR OMA; VCRYYAE; -.
DR OrthoDB; 9812625at2; -.
DR PhylomeDB; P76149; -.
DR BioCyc; EcoCyc:G6811-MONOMER; -.
DR BioCyc; MetaCyc:G6811-MONOMER; -.
DR UniPathway; UPA00733; -.
DR PRO; PR:P76149; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0036243; F:succinate-semialdehyde dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IDA:EcoliWiki.
DR GO; GO:0006527; P:arginine catabolic process; IMP:EcoCyc.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IMP:EcoliWiki.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IDA:UniProtKB.
DR GO; GO:0009447; P:putrescine catabolic process; IMP:EcoCyc.
DR CDD; cd07100; ALDH_SSADH1_GabD1; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR044148; ALDH_GabD1-like.
DR InterPro; IPR047110; GABD/Sad-like.
DR PANTHER; PTHR43217; SUCCINATE SEMIALDEHYDE DEHYDROGENASE [NAD(P)+] SAD; 1.
DR PANTHER; PTHR43217:SF1; SUCCINATE SEMIALDEHYDE DEHYDROGENASE [NAD(P)+] SAD; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..462
FT /note="Succinate semialdehyde dehydrogenase [NAD(P)+] Sad"
FT /id="PRO_0000056598"
FT ACT_SITE 234
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 268
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 136..137
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 160..163
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 212..213
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 235
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 365
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P25526"
SQ SEQUENCE 462 AA; 49718 MW; 78BEF85ED538C684 CRC64;
MTITPATHAI SINPATGEQL SVLPWAGADD IENALQLAAA GFRDWRETNI DYRAEKLRDI
GKALRARSEE MAQMITREMG KPINQARAEV AKSANLCDWY AEHGPAMLKA EPTLVENQQA
VIEYRPLGTI LAIMPWNFPL WQVMRGAVPI ILAGNGYLLK HAPNVMGCAQ LIAQVFKDAG
IPQGVYGWLN ADNDGVSQMI KDSRIAAVTV TGSVRAGAAI GAQAGAALKK CVLELGGSDP
FIVLNDADLE LAVKAAVAGR YQNTGQVCAA AKRFIIEEGI ASAFTERFVA AAAALKMGDP
RDEENALGPM ARFDLRDELH HQVEKTLAQG ARLLLGGEKM AGAGNYYPPT VLANVTPEMT
AFREEMFGPV AAITIAKDAE HALELANDSE FGLSATIFTT DETQARQMAA RLECGGVFIN
GYCASDARVA FGGVKKSGFG RELSHFGLHE FCNIQTVWKD RI
//
