ID   GABD1_MYCTO             Reviewed;         457 AA.
AC   P9WNX8; L0T5V9; P71989; Q7DA77;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
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=MT0245;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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. NAD(+)
CC       can substitute for NADP(+), but enzymatic activity is three times
CC       reduced (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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK44465.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK44465.1; ALT_INIT; Genomic_DNA.
DR   PIR; F70687; F70687.
DR   RefSeq; WP_003912534.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNX8; -.
DR   SMR; P9WNX8; -.
DR   EnsemblBacteria; AAK44465; AAK44465; MT0245.
DR   GeneID; 45424206; -.
DR   KEGG; mtc:MT0245; -.
DR   HOGENOM; CLU_005391_1_0_11; -.
DR   Proteomes; UP000001020; 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..457
FT                   /note="Succinate-semialdehyde dehydrogenase [NADP(+)] 1"
FT                   /id="PRO_0000427049"
FT   ACT_SITE        231
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        265
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         133..134
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         157..160
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         209..210
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         362
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   457 AA;  48545 MW;  B391266C5441A05F CRC64;
     MPIATINPAT GETVKTFTAA TDDEVDAAIA RAHRRFADYR QTSFAQRARW ANATADLLEA
     EADQAAAMMT LEMGKTLAAA KAEALKCAKG FRYYAENAEA LLADEPADAA KVGASAAYGR
     YQPLGVILAV MPWNFPLWQA VRFAAPALMA GNVGLLKHAS NVPQCALYLA DVIARGGFPD
     GCFQTLLVSS GAVEAILRDP RVAAATLTGS EPAGQSVGAI AGNEIKPTVL ELGGSDPFIV
     MPSADLDAAV STAVTGRVQN NGQSCIAAKR FIVHADIYDD FVDKFVARMA ALRVGDPTDP
     DTDVGPLATE QGRNEVAKQV EDAAAAGAVI RCGGKRLDRP GWFYPPTVIT DISKDMALYT
     EEVFGPVASV FRAANIDEAV EIANATTFGL GSNAWTRDET EQRRFIDDIV AGQVFINGMT
     VSYPELPFGG VKRSGYGREL SAHGIREFCN IKTVWIA