KGSD1_AZOBR
ID KGSD1_AZOBR Reviewed; 481 AA.
AC Q1JUP4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Alpha-ketoglutaric semialdehyde dehydrogenase 1;
DE Short=alphaKGSA dehydrogenase 1;
DE EC=1.2.1.26 {ECO:0000269|PubMed:16835232};
DE AltName: Full=2,5-dioxovalerate dehydrogenase 1;
DE AltName: Full=2-oxoglutarate semialdehyde dehydrogenase 1;
DE AltName: Full=KGSADH-I {ECO:0000305};
DE AltName: Full=Succinate-semialdehyde dehydrogenase [NAD(+)];
DE Short=SSDH;
DE EC=1.2.1.24;
GN Name=araE;
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 2-26; 93-97; 253-257
RP AND 339-343, FUNCTION IN ARABINOSE DEGRADATION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, DISRUPTION
RP PHENOTYPE, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=16835232; DOI=10.1074/jbc.m602585200;
RA Watanabe S., Kodaki T., Makino K.;
RT "A novel alpha-ketoglutaric semialdehyde dehydrogenase: evolutionary
RT insight into an alternative pathway of bacterial L-arabinose metabolism.";
RL J. Biol. Chem. 281:28876-28888(2006).
RN [2]
RP PATHWAY.
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=6798025; DOI=10.1128/jb.149.1.364-367.1982;
RA Novick N.J., Tyler M.E.;
RT "L-arabinose metabolism in Azospirillum brasiliense.";
RL J. Bacteriol. 149:364-367(1982).
CC -!- FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of alpha-
CC ketoglutaric semialdehyde (alphaKGSA) to alpha-ketoglutarate. Is
CC involved in a degradation pathway of L-arabinose that allows
CC A.brasilense to grow on L-arabinose as a sole carbon source. Prefers
CC NAD(+) to NADP(+) as a cosubstrate. Displays broad substrate
CC specificity: exhibits the highest activity with alphaKGSA and succinic
CC semialdehyde as substrates, but to a lesser extent, is also active with
CC glutaraldehyde, benzaldehyde, and a number of aldehydes from C3 to C8.
CC {ECO:0000269|PubMed:16835232}.
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:16835232};
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:16835232};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + succinate semialdehyde = 2 H(+) + NADH +
CC succinate; Xref=Rhea:RHEA:13217, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57706, ChEBI:CHEBI:57945; EC=1.2.1.24;
CC Evidence={ECO:0000269|PubMed:16835232};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.0 uM for alpha-ketoglutaric semialdehyde (in the presence of
CC NAD(+), at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:16835232};
CC KM=15.9 uM for alpha-ketoglutaric semialdehyde (in the presence of
CC NADP(+), at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:16835232};
CC KM=38.5 uM for succinic semialdehyde (in the presence of NAD(+), at
CC 25 degrees Celsius and pH 7.2) {ECO:0000269|PubMed:16835232};
CC KM=16.3 uM for glutaraldehyde (in the presence of NAD(+), at 25
CC degrees Celsius and pH 7.2) {ECO:0000269|PubMed:16835232};
CC Vmax=42.5 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:16835232};
CC Vmax=9.85 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:16835232};
CC Vmax=24.7 umol/min/mg enzyme for the oxidation of succinic
CC semialdehyde with NAD(+) (at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:16835232};
CC Vmax=13.9 umol/min/mg enzyme for the oxidation of glutaraldehyde with
CC NAD(+) (at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:16835232};
CC Note=The catalytic efficiency with alphaKGSA in the presence of
CC NAD(+) is 5.2- and 6.2-fold higher than with succinic semialdehyde
CC and glutaraldehyde, respectively. When NADP(+) is used as a
CC cosubstrate, the catalytic efficiency with alphaKGSA drops 6-fold
CC compared with that in the presence of NAD(+).;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16835232}.
CC -!- INDUCTION: Induced by L-arabinose, and to a lesser extent by D-glucose
CC or a nutrient-rich medium. {ECO:0000269|PubMed:16835232}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on L-
CC arabinose as a sole carbon source but grow on a nutrient-rich medium or
CC D-glucose at the same growth rate as the wild-type strain. Moreover,
CC both the wild-type and the mutant strains can grow on D-glucarate or D-
CC galactarate as a sole carbon source. {ECO:0000269|PubMed:16835232}.
CC -!- MISCELLANEOUS: A.brasilense possesses two isozymes of alphaKGSA
CC dehydrogenase with essential physiological roles for the L-arabinose
CC and D-glucarate/D-galactarate metabolisms, respectively. The L-
CC arabinose isozyme was isolated in PubMed:16835232 and is described in
CC this entry. The other NAD(+)-preferring isozyme of alphaKGSA
CC dehydrogenase is induced dramatically by D-glucarate or D-galactarate
CC but not by L-arabinose.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AB241137; BAE94276.1; -; Genomic_DNA.
DR PDB; 5X5T; X-ray; 2.25 A; A/B=2-481.
DR PDB; 5X5U; X-ray; 2.30 A; A/B=2-481.
DR PDBsum; 5X5T; -.
DR PDBsum; 5X5U; -.
DR AlphaFoldDB; Q1JUP4; -.
DR SMR; Q1JUP4; -.
DR BRENDA; 1.2.1.24; 611.
DR BRENDA; 1.2.1.26; 611.
DR SABIO-RK; Q1JUP4; -.
DR GO; GO:0047533; F:2,5-dioxovalerate dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
DR GO; GO:0070401; F:NADP+ binding; IDA:UniProtKB.
DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0019570; P:L-arabinose catabolic process to 2-oxoglutarate; IDA:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
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 Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Arabinose catabolism; Carbohydrate metabolism;
KW Direct protein sequencing; NAD; NADP; Oxidoreductase.
FT CHAIN 1..481
FT /note="Alpha-ketoglutaric semialdehyde dehydrogenase 1"
FT /id="PRO_0000418508"
FT ACT_SITE 253
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 287
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 154..155
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 178..181
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 231..232
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:5X5T"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:5X5T"
FT HELIX 45..62
FT /evidence="ECO:0007829|PDB:5X5T"
FT HELIX 67..83
FT /evidence="ECO:0007829|PDB:5X5T"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:5X5T"
FT HELIX 100..121
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:5X5U"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:5X5T"
FT HELIX 159..171
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:5X5T"
FT HELIX 185..197
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:5X5T"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:5X5T"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:5X5T"
FT HELIX 268..280
FT /evidence="ECO:0007829|PDB:5X5T"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:5X5T"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:5X5T"
FT HELIX 300..312
FT /evidence="ECO:0007829|PDB:5X5T"
FT HELIX 332..347
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:5X5T"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 387..397
FT /evidence="ECO:0007829|PDB:5X5T"
FT HELIX 398..405
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 407..417
FT /evidence="ECO:0007829|PDB:5X5T"
FT HELIX 421..430
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 434..440
FT /evidence="ECO:0007829|PDB:5X5T"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:5X5U"
FT HELIX 464..470
FT /evidence="ECO:0007829|PDB:5X5T"
FT STRAND 471..479
FT /evidence="ECO:0007829|PDB:5X5T"
SQ SEQUENCE 481 AA; 50831 MW; 9AEFB070DD8D681D CRC64;
MANVTYTDTQ LLIDGEWVDA ASGKTIDVVN PATGKPIGRV AHAGIADLDR ALAAAQSGFE
AWRKVPAHER AATMRKAAAL VRERADAIAQ LMTQEQGKPL TEARVEVLSA ADIIEWFADE
GRRVYGRIVP PRNLGAQQTV VKEPVGPVAA FTPWNFPVNQ VVRKLSAALA TGCSFLVKAP
EETPASPAAL LRAFVDAGVP AGVIGLVYGD PAEISSYLIP HPVIRKVTFT GSTPVGKQLA
SLAGLHMKRA TMELGGHAPV IVAEDADVAL AVKAAGGAKF RNAGQVCISP TRFLVHNSIR
DEFTRALVKH AEGLKVGNGL EEGTTLGALA NPRRLTAMAS VIDNARKVGA SIETGGERIG
SEGNFFAPTV IANVPLDADV FNNEPFGPVA AIRGFDKLEE AIAEANRLPF GLAGYAFTRS
FANVHLLTQR LEVGMLWINQ PATPWPEMPF GGVKDSGYGS EGGPEALEPY LVTKSVTVMA
V
