ID   GABD2_MYCTA             Reviewed;         518 AA.
AC   A5U390;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-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=MRA_1741;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
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; CP000611; ABQ73490.1; -; Genomic_DNA.
DR   RefSeq; WP_003898989.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U390; -.
DR   SMR; A5U390; -.
DR   STRING; 419947.MRA_1741; -.
DR   EnsemblBacteria; ABQ73490; ABQ73490; MRA_1741.
DR   KEGG; mra:MRA_1741; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_11; -.
DR   OMA; NWNKQLT; -.
DR   OrthoDB; 293754at2; -.
DR   Proteomes; UP000001988; 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_0000310712"
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;  55324 MW;  E3AC9E895EB46270 CRC64;
     MPAPSAEVFD RLRNLAAIKD VAARPTRTID EVFTGKPLTT IPVGTAADVE AAFAEARAAQ
     TDWAKRPVIE RAAVIRRYRD LVIENREFLM DLLQAEAGKA RWAAQEEIVD LIANANYYAR
     VCVDLLKPRK AQPLLPGIGK TTVCYQPKGV VGVISPWNYP MTLTVSDSVP ALVAGNAVVL
     KPDSQTPYCA LACAELLYRA GLPRALYAIV PGPGSVVGTA ITDNCDYLMF TGSSATGSRL
     AEHAGRRLIG FSAELGGKNP MIVARGANLD KVAKAATRAC FSNAGQLCIS IERIYVEKDI
     AEEFTRKFGD AVRNMKLGTA YDFSVDMGSL ISEAQLKTVS GHVDDATAKG AKVIAGGKAR
     PDIGPLFYEP TVLTNVAPEM ECAANETFGP VVSIYPVADV DEAVEKANDT DYGLNASVWA
     GSTAEGQRIA ARLRSGTVNV DEGYAFAWGS LSAPMGGMGL SGVGRRHGPE GLLKYTESQT
     IATARVFNLD PPFGIPATVW QKSLLPIVRT VMKLPGRR