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 24-JAN-2024, entry version 44.
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; Actinomycetota; Actinomycetes; Mycobacteriales; 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 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 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 InterPro; IPR047110; GABD/Sad-like.
DR PANTHER; PTHR43217; SUCCINATE SEMIALDEHYDE DEHYDROGENASE [NAD(P)+] SAD; 1.
DR PANTHER; PTHR43217:SF1; SUCCINATE SEMIALDEHYDE DEHYDROGENASE [NAD(P)+] SAD; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Reference proteome; 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
//
