(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 133.
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}.
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   SMR; P42236; -.
DR   STRING; 224308.BSU02470; -.
DR   jPOST; P42236; -.
DR   PaxDb; P42236; -.
DR   PRIDE; P42236; -.
DR   EnsemblBacteria; CAB12041; CAB12041; BSU02470.
DR   GeneID; 938406; -.
DR   KEGG; bsu:BSU02470; -.
DR   PATRIC; fig|224308.179.peg.254; -.
DR   eggNOG; ENOG4105C26; Bacteria.
DR   eggNOG; COG1012; LUCA.
DR   HOGENOM; HOG000271511; -.
DR   InParanoid; P42236; -.
DR   KO; K22187; -.
DR   OMA; WTRMLVH; -.
DR   PhylomeDB; P42236; -.
DR   BioCyc; BSUB:BSU02470-MONOMER; -.
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;
DR   PRODOM; P42236.
DR   SWISS-2DPAGE; P42236.
KW   NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..488
FT                   /note="Alpha-ketoglutaric semialdehyde dehydrogenase"
FT                   /id="PRO_0000056444"
FT   NP_BIND         233..238
FT                   /note="NAD(P)"
FT                   /evidence="ECO:0000250|UniProtKB:P47895"
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"
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
//

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