ID   SAPD_PSESP              Reviewed;         477 AA.
AC   H8ZPX2;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   03-MAY-2023, entry version 30.
DE   RecName: Full=3-succinoylsemialdehyde-pyridine dehydrogenase;
DE            Short=SAPD;
DE            EC=1.2.1.83;
GN   Name=ald;
OS   Pseudomonas sp.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND CATALYTIC
RP   ACTIVITY.
RC   STRAIN=HZN6;
RX   PubMed=22267672; DOI=10.1128/aem.07025-11;
RA   Qiu J., Ma Y., Wen Y., Chen L., Wu L., Liu W.;
RT   "Functional identification of two novel genes from Pseudomonas sp. strain
RT   HZN6 involved in the catabolism of nicotine.";
RL   Appl. Environ. Microbiol. 78:2154-2160(2012).
CC   -!- FUNCTION: Catalyzes the dehydrogenation of 3-succinoylsemialdehyde-
CC       pyridine to 3-succinoyl-pyridine in the nicotine degradation pathway.
CC       {ECO:0000269|PubMed:22267672}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-oxo-4-(pyridin-3-yl)butanal + H2O + NADP(+) = 4-oxo-4-
CC         (pyridin-3-yl)butanoate + 2 H(+) + NADPH; Xref=Rhea:RHEA:34215,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:66879, ChEBI:CHEBI:66942; EC=1.2.1.83;
CC         Evidence={ECO:0000269|PubMed:22267672};
CC   -!- PATHWAY: Alkaloid degradation; nicotine degradation.
CC       {ECO:0000269|PubMed:22267672}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; JN391188; AFD54464.1; -; Genomic_DNA.
DR   AlphaFoldDB; H8ZPX2; -.
DR   SMR; H8ZPX2; -.
DR   KEGG; ag:AFD54464; -.
DR   BRENDA; 1.2.1.83; 5085.
DR   UniPathway; UPA00106; -.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR   GO; GO:0019608; P:nicotine catabolic process; IDA:UniProtKB.
DR   CDD; cd07138; ALDH_CddD_SSP0762; 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   PANTHER; PTHR42804; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42804:SF1; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   NADP; Oxidoreductase.
FT   CHAIN           1..477
FT                   /note="3-succinoylsemialdehyde-pyridine dehydrogenase"
FT                   /id="PRO_0000421822"
FT   ACT_SITE        246
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   BINDING         202..208
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   477 AA;  51246 MW;  2F19D0092186445D CRC64;
     MRDYREFYID GQWVRPKGAR EAEVINPATE KIVGLISLGT EEHVDLAVRA ARRAFDGWSR
     TSKDQRLELL EQVCRAFESK LDEIAKAITE EMGAPLVQLA LPLQAPAGLG HFLTAASILR
     DYDFEESLGT TRVVREPAGV CGLITPWNWP LNQIAAKVAP ALAAGCTMVL KPSEIAPFSA
     YLLARIFDEV GVPPGVFNLV NGDGPGVGAP LAAHPEVDLV SFTGSTRAGT LVSTAAAPTV
     KRVALELGGK SANIILDDAD LETAVKHGVR TMMLNTGQSC NAPSRMLVPL SKLDEVEHLA
     EHFCKEIVVG DPMHSDTNIG PLASGMQYEK VQDCIRQGVA EGAKLICGGL GRPDGLESGY
     FAQPTIFSAV NKQMYIAREE IFGPVLCIMP YGDENEAIQI ANDSCYGLSG YVSSGSLERA
     RNVAKQLRTG AVHLNGAALD FTAPFGGYKQ SGNGREWGKY GFEEFLEIKA VMGYEGS
//