ID   GABD2_MYCUA             Reviewed;         518 AA.
AC   A0PST9;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Putative succinate-semialdehyde dehydrogenase [NADP(+)] 2;
DE            Short=SSADH 2;
DE            Short=SSDH 2;
DE            EC=1.2.1.79;
GN   Name=gabD2; OrderedLocusNames=MUL_3190;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
CC   -!- FUNCTION: Catalyzes the NADP(+)-dependent oxidation of succinate
CC       semialdehyde to succinate. Although it has succinate semialdehyde
CC       dehydrogenase activity, is likely to act physiologically on a different
CC       aldehyde(s) (By similarity). {ECO:0000250}.
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=1.2.1.79;
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000325; ABL05408.1; -; Genomic_DNA.
DR   RefSeq; WP_011741019.1; NC_008611.1.
DR   AlphaFoldDB; A0PST9; -.
DR   SMR; A0PST9; -.
DR   STRING; 362242.MUL_3190; -.
DR   EnsemblBacteria; ABL05408; ABL05408; MUL_3190.
DR   KEGG; mul:MUL_3190; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_11; -.
DR   OMA; NWNKQLT; -.
DR   Proteomes; UP000000765; Chromosome.
DR   GO; GO:0036243; F:succinate-semialdehyde dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   NADP; Oxidoreductase.
FT   CHAIN           1..518
FT                   /note="Putative succinate-semialdehyde dehydrogenase
FT                   [NADP(+)] 2"
FT                   /id="PRO_0000310713"
FT   ACT_SITE        254
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        288
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   BINDING         157..158
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         181..184
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         232..233
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         386
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   518 AA;  55236 MW;  06E2D6FEC9A43F01 CRC64;
     MPVPSSAVFE CLLSLAAIKD VDARPTRTID EVFTGKPLTT IPVGTAEDVE AAFAEAREAQ
     ANWAKRPVSE RAEVIRRYRD LVIENREFLM DLLQAEAGKA RWAAQEEVVD LVANANYYAR
     VSAGLLKPRT VQALLPGIGK TTVGYQPKGV VGVISPWNYP MTLTASDSVP ALIAGNAVVL
     KPDSQTPYCA LACAELLYRA GLPRALYAIV PGPGSVVGTA IADNCDYLMF TGSSATGSRL
     AERAGRRLIG FSAELGGKNA MIVTRGVNLD KVAKAATRAC FSNAGQLCIS IERIYVEKDI
     ADEFTRKFGD AVRSMKLGTA YDFSVDMGSL ISEGQLKTVS GHVDDATAKG AKVIAGGKAR
     PDVGPLFYEP TVLTDVTHEM ECADNETFGP LVSIYPVADV EEAVEKANDT EYGLNASVWA
     GSTPEGEKIA ARLRSGTVNV NEGYAFAWGS LSAPMGGMGI SGVGRRHGPE GLLKYTESQT
     IATARVFNLD PPMGVPPTLW QKSLLPIVRT VMKLPGRK