KGSD2_AZOBR
ID KGSD2_AZOBR Reviewed; 525 AA.
AC Q08IC0;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Alpha-ketoglutaric semialdehyde dehydrogenase 2 {ECO:0000303|PubMed:17202142};
DE Short=alphaKGSA dehydrogenase 2 {ECO:0000303|PubMed:17202142};
DE EC=1.2.1.26 {ECO:0000269|PubMed:17202142};
DE AltName: Full=2,5-dioxovalerate dehydrogenase 2 {ECO:0000305};
DE AltName: Full=KGSADH-II {ECO:0000303|PubMed:17202142};
OS Azospirillum brasilense.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15, IDENTIFICATION
RP BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, SUBUNIT, AND INDUCTION.
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=17202142; DOI=10.1074/jbc.m611057200;
RA Watanabe S., Yamada M., Ohtsu I., Makino K.;
RT "alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in
RT metabolic pathways of D-glucarate, D-galactarate, and hydroxy-L-proline.
RT Molecular and metabolic convergent evolution.";
RL J. Biol. Chem. 282:6685-6695(2007).
CC -!- FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of alpha-
CC ketoglutaric semialdehyde (alphaKGSA) to alpha-ketoglutarate. Involved
CC in D-glucarate/D-galactarate metabolism. Prefers NAD(+) to NADP(+) as a
CC cosubstrate. {ECO:0000269|PubMed:17202142}.
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:17202142};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,5-dioxopentanoate + H2O + NAD(+) = 2-oxoglutarate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:47152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58136; Evidence={ECO:0000269|PubMed:17202142};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=24.6 uM for alpha-ketoglutaric semialdehyde (in the presence of
CC NAD(+), at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:17202142};
CC KM=11 uM for alpha-ketoglutaric semialdehyde (in the presence of
CC NADP(+), at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:17202142};
CC KM=116.9 uM for NAD(+) (at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:17202142};
CC KM=62.2 uM for NADP(+) (at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:17202142};
CC Vmax=37.2 umol/min/mg enzyme for the oxidation of alpha-ketoglutaric
CC semialdehyde with NAD(+) (at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:17202142};
CC Vmax=14.8 umol/min/mg enzyme for the oxidation of alpha-ketoglutaric
CC semialdehyde with NADP(+) (at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:17202142};
CC Note=kcat is 53.9 sec(-1) with alpha-ketoglutaric semialdehyde as
CC substrate (in the presence of NAD(+)). kcat is 15.4 sec(-1) with
CC alpha-ketoglutaric semialdehyde as substrate (in the presence of
CC NADP(+)). {ECO:0000269|PubMed:17202142};
CC -!- PATHWAY: Carbohydrate acid metabolism; D-glucarate degradation.
CC {ECO:0000305|PubMed:17202142}.
CC -!- PATHWAY: Carbohydrate acid metabolism; galactarate degradation.
CC {ECO:0000305|PubMed:17202142}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17202142}.
CC -!- INDUCTION: Induced by D-glucarate and D-galactarate.
CC {ECO:0000269|PubMed:17202142}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AB275768; BAF33385.1; -; Genomic_DNA.
DR AlphaFoldDB; Q08IC0; -.
DR SMR; Q08IC0; -.
DR BRENDA; 1.2.1.26; 611.
DR SABIO-RK; Q08IC0; -.
DR UniPathway; UPA00564; -.
DR UniPathway; UPA00565; -.
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 GO; GO:0046392; P:galactarate 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 Direct protein sequencing; NAD; NADP; Oxidoreductase.
FT CHAIN 1..525
FT /note="Alpha-ketoglutaric semialdehyde dehydrogenase 2"
FT /id="PRO_0000444626"
FT ACT_SITE 266
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT ACT_SITE 303
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT BINDING 185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT BINDING 188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT BINDING 242..247
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT BINDING 394
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
SQ SEQUENCE 525 AA; 54351 MW; EB6A55B18BC948FB CRC64;
MQLTGEMLIG AEAVAGSAGT LRAFDPSKGE PIDAPVFGVA AQADVERACE LARDAFDAYR
AQPLAARAAF LEAIADEIVA LGDALIERAH AETGLPVARL QGERGRTVGQ LRLFARVVRD
GRFLAASIDP AQPARTPLPR SDLRLQKVGL GPVVVFGASN FPLAFSVAGG DTASALAAGC
PVIVKAHEAH LGTSELVGRA IRAAVAKTGM PAGVFSLLVG PGRVIGGALV SHPAVQAVGF
TGSRQGGMAL VQIANARPQP IPVYAEMSSI NPVVLFPAAL AARGDAIATG FVDSLTLGVG
QFCTNPGLVL AIDGPDLDRF ETVAAQALAK KPAGVMLTQG IADAYRNGRG KLAELPGVRE
IGAGEAAQTD CQAGGALYEV GAQAFLAEPA FSHEVFGPAS LIVRCRDLDE VARVLEALEG
QLTATLQMDA DDKPLARRLL PVLERKAGRL LVNGYPTGVE VCDAMVHGGP FPATSNPAVT
SVGATAIERF LRPVCYQDFP DDLLPEGLQE SNPLAIPRLR DGKAE
