ID   GABD_SYNY3              Reviewed;         454 AA.
AC   Q55585;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Probable succinate-semialdehyde dehydrogenase [NADP(+)];
DE            Short=SSDH;
DE            EC=1.2.1.79;
GN   Name=gabD; OrderedLocusNames=slr0370;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA10090.1; -; Genomic_DNA.
DR   PIR; S76112; S76112.
DR   AlphaFoldDB; Q55585; -.
DR   SMR; Q55585; -.
DR   IntAct; Q55585; 2.
DR   STRING; 1148.gene:10499582; -.
DR   PaxDb; 1148-1001464; -.
DR   EnsemblBacteria; BAA10090; BAA10090; BAA10090.
DR   KEGG; syn:slr0370; -.
DR   eggNOG; COG1012; Bacteria.
DR   InParanoid; Q55585; -.
DR   PhylomeDB; Q55585; -.
DR   BioCyc; MetaCyc:SGL_RS12900-MONOMER; -.
DR   UniPathway; UPA00733; -.
DR   Proteomes; UP000001425; Chromosome.
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   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
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.
PE   3: Inferred from homology;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..454
FT                   /note="Probable succinate-semialdehyde dehydrogenase
FT                   [NADP(+)]"
FT                   /id="PRO_0000056574"
FT   ACT_SITE        228
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        262
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         130..131
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         154..157
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         206..207
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         359
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   454 AA;  48749 MW;  8785B19AEF376317 CRC64;
     MAIATINPAT GQTVQTFIAH SQVEVNAKLD LAQETFQSFR HLPFAQRGQW LRKAADILEQ
     RRDEWAALMT LEMGKSIPQA IAEVNKCALV CRFYADKAEE YLADEVVTTD ASQSFIAYQP
     LGVILAVMPW NFPFWQVFRF AAPALMAGNV GLLKHASNVP QCALAIAEIF QTAGFPEGAF
     QTLLIGGKVA SELMADDRIQ AGTLTGSEPA GASFASAAAG QIKKTVLELG GSDPFIVLED
     ADLDQALKVA VPARMQNNGQ SCIAAKRFIV QASVAEEFFQ RLTKAFQALK VGDPSLSTTD
     IGPLATPDIL ADIVAQVEQT IAAGAHCRCG GQALDQPGNY YPPTLLTDVP PNAPTYRQEF
     FGPVALGFTV DNLEEAIALA NDIPFGLGAS AWTTNPENQQ KLIRGIEAGA VFINGMTKSD
     PRIPFGGIKR SGFGRELGRM GILEFVNAKT VWIA
//