ID   KGSDH_ACIAD             Reviewed;         526 AA.
AC   Q6FFQ0;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Alpha-ketoglutaric semialdehyde dehydrogenase;
DE            Short=alphaKGSA dehydrogenase;
DE            EC=1.2.1.26;
DE   AltName: Full=2,5-dioxovalerate dehydrogenase;
GN   OrderedLocusNames=ACIAD0131;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
RN   [2]
RP   FUNCTION, PATHWAY, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=18364348; DOI=10.1074/jbc.m800487200;
RA   Aghaie A., Lechaplais C., Sirven P., Tricot S., Besnard-Gonnet M.,
RA   Muselet D., de Berardinis V., Kreimeyer A., Gyapay G., Salanoubat M.,
RA   Perret A.;
RT   "New insights into the alternative D-glucarate degradation pathway.";
RL   J. Biol. Chem. 283:15638-15646(2008).
CC   -!- FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of alpha-
CC       ketoglutaric semialdehyde (alphaKGSA) to alpha-ketoglutarate in the D-
CC       glutarate degradation pathway. {ECO:0000269|PubMed:18364348}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,5-dioxopentanoate + H2O + NADP(+) = 2-oxoglutarate + 2 H(+)
CC         + NADPH; Xref=Rhea:RHEA:11296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58136,
CC         ChEBI:CHEBI:58349; EC=1.2.1.26;
CC         Evidence={ECO:0000269|PubMed:18364348};
CC   -!- PATHWAY: Carbohydrate acid metabolism; D-glucarate degradation.
CC       {ECO:0000269|PubMed:18364348}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CR543861; CAG67107.1; -; Genomic_DNA.
DR   RefSeq; WP_004930669.1; NC_005966.1.
DR   AlphaFoldDB; Q6FFQ0; -.
DR   SMR; Q6FFQ0; -.
DR   STRING; 62977.ACIAD0131; -.
DR   PRIDE; Q6FFQ0; -.
DR   EnsemblBacteria; CAG67107; CAG67107; ACIAD0131.
DR   GeneID; 45232653; -.
DR   KEGG; aci:ACIAD0131; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_027555_0_0_6; -.
DR   OMA; FKAHNAH; -.
DR   OrthoDB; 618655at2; -.
DR   BioCyc; ASP62977:ACIAD_RS00615-MON; -.
DR   BioCyc; MetaCyc:MON-15626; -.
DR   BRENDA; 1.2.1.26; 8909.
DR   SABIO-RK; Q6FFQ0; -.
DR   UniPathway; UPA00564; -.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0047533; F:2,5-dioxovalerate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0042838; P:D-glucarate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07129; ALDH_KGSADH; 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; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR044151; ALDH_KGSADH.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
PE   1: Evidence at protein level;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..526
FT                   /note="Alpha-ketoglutaric semialdehyde dehydrogenase"
FT                   /id="PRO_0000424018"
FT   ACT_SITE        264
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        301
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         159..160
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         185..188
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         240..241
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         393
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   526 AA;  56145 MW;  C2C73E0E1645A976 CRC64;
     MSENNGKQFI NGQRVAANAP TIESINATDY QPTGYLFSQA TLDEVDQAAQ AAYQAFLKYQ
     HTTQQQRADF LDEIAIQIEN LGSKLQEVAA QETGLPLVRL QGETGRVTGQ LRLFAELLRR
     GDFYGARIDT ALPERKPLPR VDLRQYKIGV GPVAVFGASN FPLAFSTAGG DTVAALAAGC
     SVVFKAHSGH MATAELVAQA IEKAILNSGI PSGTFNMIFG SRVGANLVEH PLIQAAGFTG
     SLEGGMALFN LAQNRPQPIP FFAEMSSVNP VIVMPEALNA RGEKVAQDTV ASFNMGCGQF
     CTKPGLIIGI KSPAFDQFVT ALIDTTRTAV PQIMLNQGTL KSYQQGIDAL LNEQGFKCIA
     SGQAPELISQ AQPHLFQADQ SVLLSGNPKL QHEVFGPMSI VIAVDDEATL LNGLEKLAGQ
     LTATIIADES DLPQAKELLN LLTRKAGRVL FNGFPTGVEV SDAMVHGGPF PATSDSRGTS
     VGTGAIERFL RPVCYQNTSQ VLLPDVLKDG NPLHITRLVN GVLTQN