KGSDH_BACSU
ID KGSDH_BACSU Reviewed; 488 AA.
AC P42236;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Alpha-ketoglutaric semialdehyde dehydrogenase {ECO:0000303|PubMed:17202142};
DE Short=alphaKGSA dehydrogenase {ECO:0000303|PubMed:17202142};
DE EC=1.2.1.26 {ECO:0000269|PubMed:17202142};
DE AltName: Full=2,5-dioxovalerate dehydrogenase {ECO:0000305};
GN Name=gucD {ECO:0000312|EMBL:CAB12041.1}; Synonyms=ycbD;
GN OrderedLocusNames=BSU02470;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7704254; DOI=10.1099/13500872-141-2-269;
RA Ogawa K., Akagawa E., Nakamura K., Yamane K.;
RT "Determination of a 21548 bp nucleotide sequence around the 24 degrees
RT region of the Bacillus subtilis chromosome.";
RL Microbiology 141:269-275(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
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 [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168 / 3NA;
RX PubMed=26658822; DOI=10.1007/s00253-015-7197-6;
RA Graf N., Wenzel M., Altenbuchner J.;
RT "Identification and characterization of the vanillin dehydrogenase YfmT in
RT Bacillus subtilis 3NA.";
RL Appl. Microbiol. Biotechnol. 100:3511-3521(2016).
CC -!- FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of alpha-
CC ketoglutaric semialdehyde (alphaKGSA) to alpha-ketoglutarate. Prefers
CC NADP(+) to NAD(+) as a cosubstrate. In vitro, can also use various
CC aldehydes. {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=10.4 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=2.8 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=1460 uM for propionaldehyde (in the presence of NADP(+))
CC {ECO:0000269|PubMed:17202142};
CC KM=170 uM for butylaldehyde (in the presence of NADP(+))
CC {ECO:0000269|PubMed:17202142};
CC KM=145 uM for valeraldehyde (in the presence of NADP(+))
CC {ECO:0000269|PubMed:17202142};
CC KM=81.4 uM for hexylaldehyde (in the presence of NADP(+))
CC {ECO:0000269|PubMed:17202142};
CC KM=39.3 uM for heptalaldehyde (in the presence of NADP(+))
CC {ECO:0000269|PubMed:17202142};
CC KM=35.2 uM for octylaldehyde (in the presence of NADP(+))
CC {ECO:0000269|PubMed:17202142};
CC KM=556.9 uM for NAD(+) (at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:17202142};
CC KM=94 uM for NADP(+) (at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:17202142};
CC Vmax=1.14 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=1.05 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 Vmax=0.53 umol/min/mg enzyme for the oxidation of propionaldehyde
CC with NADP(+) (at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:17202142};
CC Vmax=1.02 umol/min/mg enzyme for the oxidation of butylaldehyde with
CC NADP(+) (at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:17202142};
CC Vmax=1.34 umol/min/mg enzyme for the oxidation of valeraldehyde with
CC NADP(+) (at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:17202142};
CC Vmax=1.08 umol/min/mg enzyme for the oxidation of hexylaldehyde with
CC NADP(+) (at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:17202142};
CC Vmax=0.90 umol/min/mg enzyme for the oxidation of heptalaldehyde with
CC NADP(+) (at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:17202142};
CC Vmax=0.87 umol/min/mg enzyme for the oxidation of octylaldehyde with
CC NADP(+) (at 25 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:17202142};
CC Note=kcat is 2.75 sec(-1) with alpha-ketoglutaric semialdehyde as
CC substrate (in the presence of NAD(+)). kcat is 1.12 sec(-1) with
CC alpha-ketoglutaric semialdehyde as substrate (in the presence of
CC NADP(+)). kcat is 1.29 sec(-1) with propionaldehyde as substrate (in
CC the presence of NADP(+)). kcat is 1.35 sec(-1) with butylaldehyde as
CC substrate (in the presence of NADP(+)). kcat is 2.10 sec(-1) with
CC valeraldehyde as substrate (in the presence of NADP(+)). kcat is 1.47
CC sec(-1) with hexylaldehyde as substrate (in the presence of NADP(+)).
CC kcat is 0.87 sec(-1) with heptalaldehyde as substrate (in the
CC presence of NADP(+)). kcat is 0.97 sec(-1) with octylaldehyde as
CC substrate (in the presence of NADP(+)).
CC {ECO:0000269|PubMed:17202142};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17202142}.
CC -!- DISRUPTION PHENOTYPE: No effect on vanillin degradation.
CC {ECO:0000269|PubMed:26658822}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; D30808; BAA06468.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12041.1; -; Genomic_DNA.
DR PIR; G69752; G69752.
DR RefSeq; NP_388129.1; NC_000964.3.
DR RefSeq; WP_003246263.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; P42236; -.
DR SMR; P42236; -.
DR STRING; 224308.BSU02470; -.
DR PaxDb; P42236; -.
DR PRIDE; P42236; -.
DR EnsemblBacteria; CAB12041; CAB12041; BSU_02470.
DR GeneID; 938406; -.
DR KEGG; bsu:BSU02470; -.
DR PATRIC; fig|224308.179.peg.254; -.
DR eggNOG; COG1012; Bacteria.
DR InParanoid; P42236; -.
DR OMA; AFTASMH; -.
DR PhylomeDB; P42236; -.
DR BioCyc; BSUB:BSU02470-MON; -.
DR SABIO-RK; P42236; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0047533; F:2,5-dioxovalerate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
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; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..488
FT /note="Alpha-ketoglutaric semialdehyde dehydrogenase"
FT /id="PRO_0000056444"
FT ACT_SITE 255
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT ACT_SITE 289
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT BINDING 180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT BINDING 233..238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT BINDING 336
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT BINDING 390
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
SQ SEQUENCE 488 AA; 52415 MW; 9C37B32EF51D59B2 CRC64;
MSVITEQNTY LNFINGEWVK SQSGDMVKVE NPADVNDIVG YVQNSTAEDV ERAVTAANEA
KTAWRKLTGA ERGQYLYKTA DIMEQRLEEI AACATREMGK TLPEAKGETA RGIAILRYYA
GEGMRKTGDV IPSTDKDALM FTTRVPLGVV GVISPWNFPV AIPIWKMAPA LVYGNTVVIK
PATETAVTCA KIIACFEEAG LPAGVINLVT GPGSVVGQGL AEHDGVNAVT FTGSNQVGKI
IGQAALARGA KYQLEMGGKN PVIVADDADL EAAAEAVITG AFRSTGQKCT ATSRVIVQSG
IYERFKEKLL QRTKDITIGD SLKEDVWMGP IASKNQLDNC LSYIEKGKQE GASLLIGGEK
LENGKYQNGY YVQPAIFDNV TSEMTIAQEE IFGPVIALIK VDSIEEALNI ANDVKFGLSA
SIFTENIGRM LSFIDEIDAG LVRINAESAG VELQAPFGGM KQSSSHSREQ GEAAKDFFTA
IKTVFVKP
