(data stored in ACNUC7421 zone)

SWISSPROT: GABD_BACSU

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   11-DEC-2019, entry version 129.
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; Firmicutes; 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}.
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   SMR; P94428; -.
DR   STRING; 224308.BSU03910; -.
DR   jPOST; P94428; -.
DR   PaxDb; P94428; -.
DR   PRIDE; P94428; -.
DR   EnsemblBacteria; CAB12199; CAB12199; BSU03910.
DR   GeneID; 939976; -.
DR   KEGG; bsu:BSU03910; -.
DR   PATRIC; fig|224308.179.peg.414; -.
DR   eggNOG; ENOG4105C26; Bacteria.
DR   eggNOG; COG1012; LUCA.
DR   HOGENOM; HOG000271509; -.
DR   InParanoid; P94428; -.
DR   KO; K00135; -.
DR   OMA; WHKLIEQ; -.
DR   PhylomeDB; P94428; -.
DR   BioCyc; BSUB:BSU03910-MONOMER; -.
DR   UniPathway; UPA00733; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IBA:GO_Central.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IEA:UniProtKB-UniPathway.
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; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   InterPro; IPR010102; Succ_semiAld_DH.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR01780; SSADH; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P94428.
DR   SWISS-2DPAGE; P94428.
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..462
FT                   /note="Succinate-semialdehyde dehydrogenase [NADP(+)]"
FT                   /id="PRO_0000377373"
FT   NP_BIND         133..134
FT                   /note="NADP"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         157..160
FT                   /note="NADP"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         210..211
FT                   /note="NADP"
FT                   /evidence="ECO:0000250"
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         233
FT                   /note="NADP; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   BINDING         366
FT                   /note="NADP"
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
//

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