ID GABD_BACSU Reviewed; 462 AA.
AC P94428; Q797N5;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 27-MAR-2024, entry version 143.
DE RecName: Full=Succinate-semialdehyde dehydrogenase [NADP(+)];
DE Short=SSDH;
DE EC=1.2.1.79;
GN Name=gabD; Synonyms=ycnH; OrderedLocusNames=BSU03910;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
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 IN THE UTILIZATION OF GABA, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / SMY;
RX PubMed=12123465; DOI=10.1046/j.1365-2958.2002.03036.x;
RA Belitsky B.R., Sonenshein A.L.;
RT "GabR, a member of a novel protein family, regulates the utilization of
RT gamma-aminobutyrate in Bacillus subtilis.";
RL Mol. Microbiol. 45:569-583(2002).
RN [4]
RP INDUCTION AT LOW PH.
RC STRAIN=168 / JH642;
RX PubMed=19114526; DOI=10.1128/aem.01652-08;
RA Wilks J.C., Kitko R.D., Cleeton S.H., Lee G.E., Ugwu C.S., Jones B.D.,
RA BonDurant S.S., Slonczewski J.L.;
RT "Acid and base stress and transcriptomic responses in Bacillus subtilis.";
RL Appl. Environ. Microbiol. 75:981-990(2009).
RN [5]
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 NADP(+) dependent oxidation of succinate
CC semialdehyde to succinate. {ECO:0000269|PubMed:12123465}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) + succinate semialdehyde = 2 H(+) + NADPH +
CC succinate; Xref=Rhea:RHEA:13213, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57706,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.79;
CC -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC -!- INDUCTION: Transcriptionally regulated by GabR in the presence of GABA.
CC Up-regulated under low pH conditions and ethanol. Expression from the
CC gabD promoter was induced by growth in the presence of glutamate.
CC {ECO:0000269|PubMed:12123465, ECO:0000269|PubMed:19114526}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to use GABA as
CC sole nitrogen source (PubMed:12123465). No effect on vanillin
CC degradation (PubMed:26658822). {ECO:0000269|PubMed:12123465,
CC ECO:0000269|PubMed:26658822}.
CC -!- MISCELLANEOUS: Expressed from the major gabT promoter and from an
CC additional gabD promoter.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; D50453; BAA09022.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12199.1; -; Genomic_DNA.
DR PIR; D69764; D69764.
DR RefSeq; NP_388273.1; NC_000964.3.
DR RefSeq; WP_003246615.1; NZ_JNCM01000031.1.
DR AlphaFoldDB; P94428; -.
DR SMR; P94428; -.
DR STRING; 224308.BSU03910; -.
DR jPOST; P94428; -.
DR PaxDb; 224308-BSU03910; -.
DR EnsemblBacteria; CAB12199; CAB12199; BSU_03910.
DR GeneID; 939976; -.
DR KEGG; bsu:BSU03910; -.
DR PATRIC; fig|224308.179.peg.414; -.
DR eggNOG; COG1012; Bacteria.
DR InParanoid; P94428; -.
DR OrthoDB; 9762913at2; -.
DR PhylomeDB; P94428; -.
DR BioCyc; BSUB:BSU03910-MONOMER; -.
DR BRENDA; 1.2.1.16; 658.
DR UniPathway; UPA00733; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0036243; F:succinate-semialdehyde dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IBA:GO_Central.
DR CDD; cd07103; ALDH_F5_SSADH_GabD; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR InterPro; IPR010102; Succ_semiAld_DH.
DR NCBIfam; TIGR01780; SSADH; 1.
DR PANTHER; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43353:SF5; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..462
FT /note="Succinate-semialdehyde dehydrogenase [NADP(+)]"
FT /id="PRO_0000377373"
FT ACT_SITE 232
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 133..134
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 157..160
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 210..211
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 462 AA; 50262 MW; 56CFCFF6E0960110 CRC64;
MPDQLTVYNP ATGEEIKTIP QQSATEVEEA IERSHQAFKT WSKTSANERT SLLKKWYELI
VEHKEELADL ITKENGKPYQ EAVGEVLYGA GYIEWFAEEA KRVYGRTVPA PTTGKRIVVT
RQPVGPVAAI TPWNFPNAMI TRKAAPALAA GCTFIIKPAP DTPLSAYELA RLAYEAGIPK
DVLQVVIGDG EEIGNVFTSS PKIRKITFTG STPVGKILMK NSADTVKHVS MELGGHAPLI
VDEDADIDLA VEQAMASKYR NAGQTCVCAN RLIVHESIKD EFAAKLSEQV SKLKVGNGLE
EGVNVGPIIN KRGFEKIVSQ IDDAVEKGAK VIAGGTYDRN DDKGCYFVNP TVLTDVDTSM
NIMHEETFGP VAPIVTFSDI DEAIQLANDT PYGLAAYFFT ENYRRGIYIS ENLEYGIIGW
NDGGPSAVQA PFGGMKESGI GREGGSEGIE PYLETKYLSI GL
//
