SSDH_PAENI
ID SSDH_PAENI Reviewed; 450 AA.
AC Q8GAI8;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Succinate-semialdehyde dehydrogenase;
DE Short=SsaDH;
DE EC=1.2.1.16;
GN Name=sad; ORFNames=ORF58;
OS Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans).
OG Plasmid pAO1.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=29320;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49919 / DSM 420 / JCM 3874 / NBRC 15511; PLASMID=pAO1;
RX PubMed=12618462; DOI=10.1128/jb.185.6.1976-1986.2003;
RA Igloi G.L., Brandsch R.;
RT "Sequence of the 165-kilobase catabolic plasmid pAO1 from Arthrobacter
RT nicotinovorans and identification of a pAO1-dependent nicotine uptake
RT system.";
RL J. Bacteriol. 185:1976-1986(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS,
RP SUBUNIT, PATHWAY, AND INDUCTION.
RX PubMed=16689938; DOI=10.1111/j.1742-4658.2006.05173.x;
RA Chiribau C.B., Mihasan M., Ganas P., Igloi G.L., Artenie V., Brandsch R.;
RT "Final steps in the catabolism of nicotine.";
RL FEBS J. 273:1528-1536(2006).
CC -!- FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of succinate
CC semialdehyde to succinate, which may enter the citric acid cycle. Is
CC involved in the catabolism of 4-methylaminobutanoate produced from
CC nicotine. Acts preferentially with NADP(+) as cosubstrate but can also
CC use NAD(+). To a lesser extent, is active also towards butyraldehyde
CC (8.5% of the activity observed with succinate semialdehyde) and
CC propionaldehyde (1.6% of the activity observed with succinate
CC semialdehyde) as substrates. {ECO:0000269|PubMed:16689938}.
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:16689938};
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:16689938};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.34 mM for succinate semialdehyde {ECO:0000269|PubMed:16689938};
CC KM=0.13 mM for NADP(+) {ECO:0000269|PubMed:16689938};
CC Note=kcat is 23000 sec(-1) with NADP(+) as cosubstrate.;
CC -!- PATHWAY: Alkaloid degradation; nicotine degradation.
CC {ECO:0000269|PubMed:16689938}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16689938}.
CC -!- INDUCTION: Is transcribed only in the presence of nicotine.
CC {ECO:0000269|PubMed:16689938}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AJ507836; CAD47916.1; -; Genomic_DNA.
DR RefSeq; WP_016359427.1; NC_021229.1.
DR RefSeq; YP_007988742.1; NC_021229.1.
DR AlphaFoldDB; Q8GAI8; -.
DR SMR; Q8GAI8; -.
DR UniPathway; UPA00106; -.
DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0036243; F:succinate-semialdehyde dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0019608; P:nicotine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW NAD; NADP; Oxidoreductase; Plasmid.
FT CHAIN 1..450
FT /note="Succinate-semialdehyde dehydrogenase"
FT /id="PRO_0000429429"
FT ACT_SITE 219
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 253
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT BINDING 119..120
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 143..146
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 197..198
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 120
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 450 AA; 47401 MW; 25711CF7C8ED38AF CRC64;
MLATLASATS EDAVAALEAA CAAQTSWART APRVRAEILR RAFDLVTARS EDFALLMTLE
MGKPLAEARG EVAYGAEFLR WFSEETVRDY GRYLTTPEGK NKILVQHKPV GPCLLITPWN
FPLAMATRKV APAVAAGCTM VLKPAKLTPL TSQLFAQTMM EAGLPAGVLN VVSSSSASGI
SGPLLKDSRL RKVSFTGSTP VGKRLMSDAS RHVLRTSMEL GGNAPFVVFE DADLDKAVEG
AMAAKMRNMG EACTAANRFL VQESVAQEFT RKFAAAMGAL STGRGTDPAS QVGPLINNGA
RDDIHALVTA AVDAGAVAVT GGAPVDGPGY FYQPTVLADV PNNAAILGQE IFGPVAPVTT
FTTEQDAIKL ANASEYGLAA YLYSRDFNRL LRVAEQIEFG MVGFNAGIIS NAAAPFGGVK
QSGLGREGGS EGIAEYTTTQ YIGIADPYEN
