ID   GABD1_MYCUA             Reviewed;         458 AA.
AC   A0PN13;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Succinate-semialdehyde dehydrogenase [NADP(+)] 1;
DE            Short=SSADH 1;
DE            Short=SSDH 1;
DE            EC=1.2.1.79;
GN   Name=gabD1; OrderedLocusNames=MUL_1153;
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. It is believed to be the main source of
CC       succinate semialdehyde dehydrogenase activity in Mycobacterium (By
CC       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; ABL03732.1; -; Genomic_DNA.
DR   RefSeq; WP_011739354.1; NC_008611.1.
DR   AlphaFoldDB; A0PN13; -.
DR   SMR; A0PN13; -.
DR   STRING; 362242.MUL_1153; -.
DR   EnsemblBacteria; ABL03732; ABL03732; MUL_1153.
DR   KEGG; mul:MUL_1153; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_2_11; -.
DR   OMA; KAMRWYA; -.
DR   Proteomes; UP000000765; Chromosome.
DR   GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro.
DR   GO; GO:0036243; F:succinate-semialdehyde dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd07100; ALDH_SSADH1_GabD1; 1.
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; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR044148; ALDH_GabD1-like.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   3: Inferred from homology;
KW   NADP; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN           1..458
FT                   /note="Succinate-semialdehyde dehydrogenase [NADP(+)] 1"
FT                   /id="PRO_0000310707"
FT   ACT_SITE        232
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        266
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         134..135
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         158..161
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         210..211
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         363
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   458 AA;  48528 MW;  FC438444970FDF85 CRC64;
     MPIATTNPAT GETVKTFTAA SNDEVDAAIA RAYARFQDYR RNTTFAQRAE WAHATADLIE
     AEADQTAALM TLEMGKTIAS AKAEVLKSAK GFRYYADNAA ALLADEPADA GKVGASQAYT
     RYQPLGVVLA VMPWNFPLWQ AGRFAAPALM AGNVGLLKHA SNVPQSALYL ADVIARAGFP
     DGCFQTLLVS ASAVEGILRD PRVAAATLTG SEPAGQSVGA IAGDEIKPTV LELGGSDPFI
     VMPSADLDKA VSTAVTGRVQ NNGQSCIAAK RFIAHADIYD AFVDKFVEQM SALTVGDPTD
     PQTQVGPLAT EQSRDEIAQQ VDDAAAAGAV IRCGGKPLAG PGWYYPPTVI TDITKDMNLY
     TEEVFGPVAS VYRAADIDEA IEIANATTFG LGSNAWTQDE AEQRRFINDI EAGQVFINGM
     TVSYPELPFG GIKRSGYGRE LAGHGIREFC NIKTVWVG