ID   DHE2_BACSU              Reviewed;         424 AA.
AC   P39633; Q53548; Q5W7E9;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
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=rocG; Synonyms=yweB; OrderedLocusNames=BSU37790;
GN   ORFNames=ipa-75d;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=95020537; PubMed=7934828;
RX   DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA   Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W.,
RA   Hullo M.-F., Ionescu M., Lubochinsky B., Marcelino L., Moszer I.,
RA   Presecan E., Santana M., Schneider E., Schweizer J., Vertes A.,
RA   Rapoport G., Danchin A.;
RT   "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT   region from 325 degrees to 333 degrees.";
RL   Mol. Microbiol. 10:371-384(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ISW1214;
RA   Khan M.H., Itoh K., Kim H., Ashida H., Ishikawa T., Shibata H.,
RA   Sawa Y.;
RT   "Low thermostability of the NAD+ specific glutamate dehydrogenase from
RT   Bacillus subtilis ISW1214: cloning, purification and
RT   characterization.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 418-424.
RX   MEDLINE=96004700; PubMed=7565595; DOI=10.1007/BF02191600;
RA   Klingel U., Miller C.M., North A.K., Stockley P.G., Baumberg S.;
RT   "A binding site for activation by the Bacillus subtilis AhrC protein,
RT   a repressor/activator of arginine metabolism.";
RL   Mol. Gen. Genet. 248:329-340(1995).
RN   [5]
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: Catabolic GlutDH involved in the utilization of
CC       glutamate and other amino acids of the glutamate family.
CC   -!- CATALYTIC ACTIVITY: L-glutamate + H(2)O + NAD(+) = 2-oxoglutarate
CC       + NH(3) + NADH.
CC   -!- INDUCTION: By arginine, ornithine or proline.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
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DR   EMBL; X73124; CAA51631.1; -; Genomic_DNA.
DR   EMBL; AB194695; BAD69594.1; -; Genomic_DNA.
DR   EMBL; Z99123; CAB15806.1; -; Genomic_DNA.
DR   EMBL; S79622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A70055; A70055.
DR   RefSeq; NP_391659.1; -.
DR   HSSP; P80319; 1GTM.
DR   IntAct; P39633; -.
DR   GeneID; 937066; -.
DR   GenomeReviews; AL009126_GR; BSU37790.
DR   KEGG; bsu:BSU37790; -.
DR   NMPDR; fig|224308.1.peg.3785; -.
DR   SubtiList; BG10621; rocG.
DR   HOGENOM; P39633; -.
DR   BioCyc; BSUB224308:BSU3776-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    424       NAD-specific glutamate dehydrogenase.
FT                                /FTId=PRO_0000182735.
FT   ACT_SITE    116    116       By similarity.
FT   CONFLICT    324    324       R -> A (in Ref. 2; BAD69594).
FT   CONFLICT    419    424       RFRGWV -> FPRMGLI (in Ref. 1; CAA51631).
SQ   SEQUENCE   424 AA;  46638 MW;  DFE311C72BEA8091 CRC64;
     MSAKQVSKDE EKEALNLFLS TQTIIKEALR KLGYPGDMYE LMKEPQRMLT VRIPVKMDNG
     SVKVFTGYRS QHNDAVGPTK GGVRFHPEVN EEEVKALSIW MTLKCGIANL PYGGGKGGII
     CDPRTMSFGE LERLSRGYVR AISQIVGPTK DIPAPDVYTN SQIMAWMMDE YSRLREFDSP
     GFITGKPLVL GGSQGRETAT AQGVTICIEE AVKKKGIKLQ NARIIIQGFG NAGSFLAKFM
     HDAGAKVIGI SDANGGLYNP DGLDIPYLLD KRDSFGMVTN LFTDVITNEE LLEKDCDILV
     PAAISNQITA KNAHNIQASI VVERANGPTT IDATKILNER GVLLVPDILA SAGGVTVSYF
     EWVQNNQGYY WSEEEVAEKL RSVMVSSFET IYQTAATHKV DMRLAAYMTG IRKSAEASRF
     RGWV
//