ID   GABD1_MYCA1             Reviewed;         472 AA.
AC   A0QMB9;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Succinate-semialdehyde dehydrogenase [NADP(+)];
DE            Short=SSADH;
DE            Short=SSDH;
DE            EC=1.2.1.79;
GN   Name=gabD1; OrderedLocusNames=MAV_4936;
OS   Mycobacterium avium (strain 104).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=243243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000479; ABK64449.1; -; Genomic_DNA.
DR   RefSeq; WP_009979644.1; NC_008595.1.
DR   AlphaFoldDB; A0QMB9; -.
DR   SMR; A0QMB9; -.
DR   EnsemblBacteria; ABK64449; ABK64449; MAV_4936.
DR   GeneID; 66696006; -.
DR   KEGG; mav:MAV_4936; -.
DR   HOGENOM; CLU_005391_5_1_11; -.
DR   OMA; KAMRWYA; -.
DR   OrthoDB; 384611at2; -.
DR   Proteomes; UP000001574; 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..472
FT                   /note="Succinate-semialdehyde dehydrogenase [NADP(+)]"
FT                   /id="PRO_0000310700"
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   472 AA;  50010 MW;  39C4E3CBCDD495C5 CRC64;
     MPIATINPAT GETVKTFTPA SDAEVDAAIA RAYERFLDYR HSTTFAQRAQ WANATADLLE
     AEADEVAAMM TLEMGKTLKS AKAEALKCAK GFRYYAQNAE QLLADEPADA GKVGAARAYI
     RYQPLGVVLA VMPWNFPLWQ AVRFAAPALM AGNVGILKHA SNVPQSALYL ADVITRGGFP
     EGCFQTLLVP SSAVERILRD PRVAAATLTG SEPAGQSVAA IAGDEIKPTV LELGGSDPFI
     VMPSADLDEA VKTAVTARVQ NNGQSCIAAK RFIVHTDIYD TFVDKFVEQM KALKVGDPTD
     PATDVGPLAT ESGRDEIAKQ VDDAVAAGAT LRCGGKPLDG PGWFYPPTVV TDITKDMALY
     TEEVFGPVAS MYRAADIDEA IEIANATTFG LGSNAWTNDA AEQQRFIDDI EAGQVFINGM
     TVSYPELGFG GVKRSGYGRE LAGLGIRAFC NAKTVWIGSS KSGDAGGGSK VE