GABD1_MYCLE
ID GABD1_MYCLE Reviewed; 457 AA.
AC O69497;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Succinate-semialdehyde dehydrogenase [NADP(+)];
DE Short=SSADH;
DE Short=SSDH;
DE EC=1.2.1.79;
GN Name=gabD1; OrderedLocusNames=ML2573; ORFNames=MLCB1883.11c;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; AL022486; CAA18560.1; -; Genomic_DNA.
DR EMBL; AL583926; CAC32105.1; -; Genomic_DNA.
DR PIR; T44871; T44871.
DR RefSeq; NP_302648.1; NC_002677.1.
DR RefSeq; WP_010908967.1; NC_002677.1.
DR AlphaFoldDB; O69497; -.
DR SMR; O69497; -.
DR STRING; 272631.ML2573; -.
DR EnsemblBacteria; CAC32105; CAC32105; CAC32105.
DR KEGG; mle:ML2573; -.
DR PATRIC; fig|272631.5.peg.4945; -.
DR Leproma; ML2573; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_5_3_11; -.
DR OMA; KAMRWYA; -.
DR Proteomes; UP000000806; 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; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..457
FT /note="Succinate-semialdehyde dehydrogenase [NADP(+)]"
FT /id="PRO_0000310703"
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; 48879 MW; 1EEF6444A6DD13BD CRC64;
MSIATINPAT GETVKTFTPT TQDEVEDAIA RAYARFDNYR HTTFTQRAKW ANATADLLEA
EANQSAALMT LEMGKTLQSA KDEAMKCAKG FRYYAEKAET LLADEPAEAA AVGASKALAR
YQPLGVVLAV MPWNFPLWQT VRFAAPALMA GNVGLLKHAS NVPQCALYLA DVIARGGFPE
DCFQTLLISA NGVEAILRDP RVAAATLTGS EPAGQAVGAI AGNEIKPTVL ELGGSDPFIV
MPSADLDAAV ATAVTGRVQN NGQSCIAAKR FIAHADIYDE FVEKFVARME TLRVGDPTDP
DTDVGPLATE SGRAQVEQQV DAAAAAGAVI RCGGKRPDRP GWFYPPTVIT DITKDMALYT
DEVFGPVASV YCATNIDDAI EIANATPFGL GSNAWTQNES EQRHFIDNIV AGQVFINGMT
VSYPELPFGG IKRSGYGREL STHGIREFCN IKTVWIA
