KGSD3_AZOBR
ID KGSD3_AZOBR Reviewed; 530 AA.
AC Q08IB7;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Alpha-ketoglutaric semialdehyde dehydrogenase 3 {ECO:0000303|PubMed:17202142};
DE Short=alphaKGSA dehydrogenase 3 {ECO:0000303|PubMed:17202142};
DE EC=1.2.1.26 {ECO:0000269|PubMed:17202142};
DE AltName: Full=2,5-dioxovalerate dehydrogenase 3 {ECO:0000305};
DE AltName: Full=KGSADH-III {ECO:0000303|PubMed:17202142};
GN Name=LhpG {ECO:0000312|EMBL:BAN78530.1};
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RA Watanabe S., Hiraoka Y., Tanimoto Y., Tozawa Y., Watanabe Y.;
RT "Characterization of D-hydroxyproline dehydrogenase from Azospirillum
RT brasilense and application for enzymatic determination of L-
RT hydroxyproline.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of alpha-
CC ketoglutaric semialdehyde (alphaKGSA) to alpha-ketoglutarate. Involved
CC in hydroxy-L-proline metabolism. Prefers NADP(+) to NAD(+) 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=6.5 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=7.5 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=1.136 mM for NAD(+) (at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:17202142};
CC KM=0.0149 mM for NADP(+) (at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:17202142};
CC Vmax=30.7 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=16.4 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 21.3 sec(-1) with alpha-ketoglutaric semialdehyde as
CC substrate (in the presence of NAD(+)). kcat is 23.0 sec(-1) with
CC alpha-ketoglutaric semialdehyde as substrate (in the presence of
CC NADP(+)). {ECO:0000269|PubMed:17202142};
CC -!- PATHWAY: Amino-acid degradation. {ECO:0000305|PubMed:17202142}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17202142}.
CC -!- INDUCTION: Induced by hydroxy-L-proline. {ECO:0000269|PubMed:17202142}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AB275769; BAF33388.1; -; Genomic_DNA.
DR EMBL; AB845355; BAN78530.1; -; Genomic_DNA.
DR AlphaFoldDB; Q08IB7; -.
DR SMR; Q08IB7; -.
DR BRENDA; 1.2.1.26; 611.
DR SABIO-RK; Q08IB7; -.
DR GO; GO:0047533; F:2,5-dioxovalerate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
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..530
FT /note="Alpha-ketoglutaric semialdehyde dehydrogenase 3"
FT /id="PRO_0000444627"
FT ACT_SITE 265
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT ACT_SITE 302
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT BINDING 184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT BINDING 241..246
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT BINDING 392
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
SQ SEQUENCE 530 AA; 55185 MW; 8B83A9E791FAD4F1 CRC64;
MQLTGHLLIG QSAIAGQNGT LHAIAAATGE PLDPAFGGAS LHDLDTACAL ADDAFDTYRD
TSLEARAAFL DAIGRHIMAL GDELIERCVI ETGLPRARIE GERGRTVGQL ALFASLVRDG
GFLDARIDPA RPERKPLPRV DLRLRNIAVG PVAVFGASNF PLAFSVAGGD TASALAAGCP
VIVKAHSAHP GTSALVGRAI QQAARECGMP AGVFSLLFDA SREIGQALVA DPRIKAVGFT
GSRRGGVALM HIAAARPEPI PVYAEMSSIN PVLLLPAALD ARHDAIAPQF VASLTLGAGQ
FCTNPGLVLA VDGPALRAFE EAAAAAVRAA PAQTMLTPHI HASYEQGVAA LRDHAAVELL
AQGAEGNRLQ ARAALLATSA EAFITHPELR DEVFGPASLI VRCPDADTLH RVLKSLEGQL
TIAAHLADGD APLFAALRPL LERKAGRILV NGFGTGVEVG HAMVHGGPFP ATSDTRTTSV
GARAIERFLR PVSYQDLPDA LLPEAIRSGN PLNVPQRIDG VPAPREANHV
