ID   GABD2_MYCS2             Reviewed;         517 AA.
AC   A0R4Q0; I7GF38;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Putative succinate-semialdehyde dehydrogenase [NADP(+)];
DE            Short=SSADH;
DE            Short=SSDH;
DE            EC=1.2.1.79;
GN   Name=gabD2; OrderedLocusNames=MSMEG_5912, MSMEI_5752;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
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; CP000480; ABK69825.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP42186.1; -; Genomic_DNA.
DR   RefSeq; WP_003897308.1; NZ_SIJM01000017.1.
DR   RefSeq; YP_890138.1; NC_008596.1.
DR   AlphaFoldDB; A0R4Q0; -.
DR   SMR; A0R4Q0; -.
DR   STRING; 246196.MSMEI_5752; -.
DR   PRIDE; A0R4Q0; -.
DR   EnsemblBacteria; ABK69825; ABK69825; MSMEG_5912.
DR   EnsemblBacteria; AFP42186; AFP42186; MSMEI_5752.
DR   GeneID; 66737199; -.
DR   KEGG; msg:MSMEI_5752; -.
DR   KEGG; msm:MSMEG_5912; -.
DR   PATRIC; fig|246196.19.peg.5752; -.
DR   eggNOG; COG1012; Bacteria.
DR   OMA; NWNKQLT; -.
DR   OrthoDB; 293754at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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; Reference proteome.
FT   CHAIN           1..517
FT                   /note="Putative succinate-semialdehyde dehydrogenase
FT                   [NADP(+)]"
FT                   /id="PRO_0000310710"
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   517 AA;  54992 MW;  8015E38D33E866C4 CRC64;
     MPAPSAADFA RLRSLVAIED LDARQSRPIE EVFTGRELTT IPVGTAEDVA AAFAKARAAQ
     RGWAHRPVAE RAAIMERFRD LVAKNRDFLM DVAQAETGKA RSAAQEEIVD MMLNARYYAR
     QAVKLLAPKR VQGLLPGVVK TVVNHHPKGV VGVISPWNYP MALSISDSIP ALLAGNAVVV
     KPDSQTPYCT LANAELLYEA GLPRDLFAVV PGPGSVVGTA IVENCDYLMF TGSTATGRTL
     AEQCGRRLIG FSAELGGKNP MIVTRGAKLD VAAKAATRAC FSNAGQLCIS IERIYVERAV
     ADEFTAKFGE QVRSMRLAAT YDFTADMGSL ISEDQIKTVS GHVDDAKAKG ATVIAGGNIR
     PDIGPRFYEP TVLTGVTDEM ECARNETFGP VVSIYPVESV AEAIEKANDT EYGLNASVWA
     GSKTEGEAIA AQLQAGTVNV DEGYALAFGS TAAPMGGMKA SGVGRRHGAD GILKYTESQT
     VATSRVLNLD PPLGISGTLW QKAMTPMIRA VQKLPGR