ID   GUDB_BACSU              Reviewed;         426 AA.
AC   P50735;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-NOV-2008, entry version 60.
DE   RecName: Full=NAD-specific glutamate dehydrogenase;
DE            Short=NAD-GDH;
DE            EC=1.4.1.2;
GN   Name=gudB; Synonyms=ypcA; OrderedLocusNames=BSU22960;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg;
RX   MEDLINE=96349105; PubMed=8760912;
RA   Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA   Serror P.;
RT   "Sequence analysis of the Bacillus subtilis chromosome region between
RT   the serA and kdg loci cloned in a yeast artificial chromosome.";
RL   Microbiology 142:2005-2016(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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   CHARACTERIZATION.
RX   MEDLINE=99047577; PubMed=9829940;
RA   Belitsky B.R., Sonenshein A.L.;
RT   "Role and regulation of Bacillus subtilis glutamate dehydrogenase
RT   genes.";
RL   J. Bacteriol. 180:6298-6305(1998).
CC   -!- FUNCTION: The wild-type version has little or no activity.
CC   -!- CATALYTIC ACTIVITY: L-glutamate + H(2)O + NAD(+) = 2-oxoglutarate
CC       + NH(3) + NADH.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
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DR   EMBL; L47648; AAC83953.1; -; Genomic_DNA.
DR   EMBL; Z99115; CAB14212.1; -; Genomic_DNA.
DR   PIR; G69933; G69933.
DR   RefSeq; NP_390177.1; -.
DR   HSSP; P80319; 1GTM.
DR   GeneID; 938975; -.
DR   GenomeReviews; AL009126_GR; BSU22960.
DR   KEGG; bsu:BSU22960; -.
DR   NMPDR; fig|224308.1.peg.2300; -.
DR   SubtiList; BG11435; gudB.
DR   HOGENOM; P50735; -.
DR   BioCyc; BSUB224308:BSU2295-MON; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004352; F:glutamate dehydrogenase activity; IEA:EC.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val_DHase.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DHase_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val_DHase_dimer.
DR   InterPro; IPR014362; Glu_DHase.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR11606:SF2; GLFV_DH; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000185; Glu_DH; 1.
DR   PRINTS; PR00082; GLFDHDRGNASE.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    426       NAD-specific glutamate dehydrogenase.
FT                                /FTId=PRO_0000182736.
FT   ACT_SITE    118    118       By similarity.
FT   VARIANT      96     98       Missing (in spontaneous mutant gudB1;
FT                                restores activity).
SQ   SEQUENCE   426 AA;  47212 MW;  5624F2DE93333E86 CRC64;
     MAADRNTGHT EEDKLDVLKS TQTVIHKALE KLGYPEEVYE LLKEPMRLLT VKIPVRMDDG
     SVKIFTGYRA HNDSVGPTKG GIRFHPNVTE KEVKAVKALS IWMSLKCGII DLPYGGGKGG
     IVCDPRDMSF RELERLSRGY VRAISQIVGP TKDVPAPDVF TNSQIMAWMM DEYSRIDEFN
     SPGFITGKPL VLGGSHGRES ATAKGVTICI KEAAKKRGID IKGARVVVQG FGNAGSYLAK
     FMHDAGAKVV GISDAYGGLY DPEGLDIDYL LDRRDSFGTV TKLFNDTITN QELLELDCDI
     LVPAAIENQI TEENAHNIRA KIVVEAANGP TTLEGTKILS DRDILLVPDV LASAGGVTVS
     YFEWVQNNQG FYWSEEEVEE KLEKMMVKSF NNIYEMANNR RIDMRLAAYM VGVRKMAEAS
     RFRGWI
//