GABD1_MYCBO
ID GABD1_MYCBO Reviewed; 457 AA.
AC Q7U2I0; A0A1R3XUW7; X2BEB3;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Succinate-semialdehyde dehydrogenase [NADP(+)] 1;
DE Short=SSADH 1;
DE Short=SSDH 1;
DE EC=1.2.1.16;
GN Name=gabD1; OrderedLocusNames=BQ2027_MB0239C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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 + NAD(+) + succinate semialdehyde = 2 H(+) + NADH +
CC succinate; Xref=Rhea:RHEA:13217, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57706, ChEBI:CHEBI:57945; EC=1.2.1.16;
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=1.2.1.16;
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=SIT98735.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; LT708304; SIT98735.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003912534.1; NC_002945.4.
DR AlphaFoldDB; Q7U2I0; -.
DR SMR; Q7U2I0; -.
DR GeneID; 45424206; -.
DR PATRIC; fig|233413.5.peg.266; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro.
DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0036243; F:succinate-semialdehyde dehydrogenase (NADP+) activity; IEA:RHEA.
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_0000310701"
FT ACT_SITE 231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 209..214
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