ID   GABD_DEIRA              Reviewed;         477 AA.
AC   O32507;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Succinate-semialdehyde dehydrogenase [NADP(+)];
DE            Short=SSDH;
DE            EC=1.2.1.79;
GN   Name=ssdA; OrderedLocusNames=DR_A0343;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KD8301;
RA   Narumi I., Kong X., Du Z., Cherdchu K., Kitayama S., Watanabe H.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
CC   -!- FUNCTION: Catalyzes the NADP(+) dependent oxidation of succinate
CC       semialdehyde to succinate. {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   -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB003475; BAA21377.1; -; Genomic_DNA.
DR   EMBL; AE001825; AAF12439.1; -; Genomic_DNA.
DR   PIR; C75589; C75589.
DR   RefSeq; NP_285666.1; NC_001264.1.
DR   RefSeq; WP_010889602.1; NZ_CP015082.1.
DR   AlphaFoldDB; O32507; -.
DR   SMR; O32507; -.
DR   STRING; 243230.DR_A0343; -.
DR   EnsemblBacteria; AAF12439; AAF12439; DR_A0343.
DR   KEGG; dra:DR_A0343; -.
DR   PATRIC; fig|243230.17.peg.3235; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_0; -.
DR   InParanoid; O32507; -.
DR   OMA; PVAHHVC; -.
DR   OrthoDB; 384611at2; -.
DR   UniPathway; UPA00733; -.
DR   Proteomes; UP000002524; Chromosome II.
DR   GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro.
DR   GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0036243; F:succinate-semialdehyde dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IEA:UniProtKB-UniPathway.
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.
FT   CHAIN           1..477
FT                   /note="Succinate-semialdehyde dehydrogenase [NADP(+)]"
FT                   /id="PRO_0000056571"
FT   ACT_SITE        240
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        274
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         142..143
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         166..169
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         218..219
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         241
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         371
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   477 AA;  51240 MW;  07A9D8B893F66AA7 CRC64;
     MTATPQASAR PERPFATVNP YTGETVKTFP FLESAEIPAL IERADQAYRE WGQRPVTERA
     AIMRRAAELM LERTDELASL ITLEMGKLLR EAKGEVALAA SILNYYGEQG PSFLEPKTIP
     VPQGEAAVLH APLGVLLGIE PWNYPLYQVV RFAAPNLVVG NTVLLKHSEL CPQSALALEQ
     LFHDAGVPQG AYTNLFLRIA DIEQVIAHPA VQGVSLTGSE RAGASVAELA GRHLKKCVLE
     LGGSDPFIVL DAEDLDTTVK AAATGRLSNT GQACIAAKRL MVVDDLYDEF VSRLGQTFSA
     FVPGDPADPS TRLGPLSSEQ AARDLQAQVQ DAIDKGATVV AGGQRPEHPG AFVQPTVLTD
     VTPDMRAYHE ELFGPVAVVY RVRDEDEAVA LANASTYGLG GAVFSSDLDR AQRVAERLDT
     GMVWINHPTS SAADLPFGGV KRSGFGRELS SMGMLEFTNQ KLVRAFPTKQ KPAQVAG