ID   DHE2_MYCS2              Reviewed;        1594 AA.
AC   A0R1C2; I7GDY4;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=NAD-specific glutamate dehydrogenase;
DE            Short=NAD-GDH;
DE            EC=1.4.1.2;
DE   AltName: Full=NAD(+)-dependent glutamate dehydrogenase;
GN   Name=gdh; OrderedLocusNames=MSMEG_4699, MSMEI_4582;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND INTERACTION WITH GARA.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=19019160; DOI=10.1111/j.1365-2958.2008.06489.x;
RA   O'Hare H.M., Duran R., Cervenansky C., Bellinzoni M., Wehenkel A.M.,
RA   Pritsch O., Obal G., Baumgartner J., Vialaret J., Johnsson K., Alzari P.M.;
RT   "Regulation of glutamate metabolism by protein kinases in mycobacteria.";
RL   Mol. Microbiol. 70:1408-1423(2008).
CC   -!- FUNCTION: Catalyzes the reversible conversion of L-glutamate to 2-
CC       oxoglutarate. Highly specific for NAD. {ECO:0000269|PubMed:19019160}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH +
CC         NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.2;
CC         Evidence={ECO:0000269|PubMed:19019160};
CC   -!- ACTIVITY REGULATION: Activity is inhibited by unphosphorylated GarA.
CC       Stimulated by manganese and magnesium. {ECO:0000269|PubMed:19019160}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=45 mM for ammonium {ECO:0000269|PubMed:19019160};
CC       pH dependence:
CC         Optimum pH is 8.5. {ECO:0000269|PubMed:19019160};
CC   -!- SUBUNIT: Interacts with (unphosphorylated) GarA.
CC       {ECO:0000269|PubMed:19019160}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AFP41034.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000480; ABK72988.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP41034.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011730019.1; NZ_SIJM01000004.1.
DR   RefSeq; YP_888960.1; NC_008596.1.
DR   PDB; 7A1D; EM; 4.19 A; A/B/C/D=1-1594.
DR   PDB; 7JSR; X-ray; 6.27 A; A/B=1-1594.
DR   PDBsum; 7A1D; -.
DR   PDBsum; 7JSR; -.
DR   AlphaFoldDB; A0R1C2; -.
DR   SMR; A0R1C2; -.
DR   IntAct; A0R1C2; 2.
DR   STRING; 246196.MSMEI_4582; -.
DR   EnsemblBacteria; ABK72988; ABK72988; MSMEG_4699.
DR   EnsemblBacteria; AFP41034; AFP41034; MSMEI_4582.
DR   GeneID; 66736015; -.
DR   KEGG; msg:MSMEI_4582; -.
DR   KEGG; msm:MSMEG_4699; -.
DR   PATRIC; fig|246196.19.peg.4589; -.
DR   eggNOG; COG2902; Bacteria.
DR   OMA; HLHINTA; -.
DR   OrthoDB; 79339at2; -.
DR   BRENDA; 1.4.1.2; 3512.
DR   SABIO-RK; A0R1C2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:InterPro.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR028971; NAD-GDH.
DR   InterPro; IPR007780; NAD_Glu_DH_bac.
DR   PANTHER; PTHR43403; PTHR43403; 1.
DR   Pfam; PF05088; Bac_GDH; 1.
DR   PIRSF; PIRSF036761; GDH_Mll4104; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
PE   1: Evidence at protein level;
KW   3D-structure; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..1594
FT                   /note="NAD-specific glutamate dehydrogenase"
FT                   /id="PRO_0000419535"
FT   ACT_SITE        816
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1594 AA;  174095 MW;  3B3C5F350E829840 CRC64;
     MIRRLSVAFL STYRGPQADA PGVTSTGPLA VAAHDDLVSD DLVAAHYRLA SMRAPGETKA
     AVYPGDAGSG AALQIVTDQA PMLVDSVTVL LHRHGIAYTA IMNPVFRVRR GLDGELLDVR
     PAAEAAPGDG ADECWILVPI TAAADGEALT EATRLVPGIL AEARQIGLDS GAMIAALHGL
     ANDLATDLEG HFPNAERKEV AALLRWLADG HFVLLGYQQC VVGDGNAEVD PASRLGVLRL
     RNDVLPPLTD SDDLLVLAQA TMPSYLRYGA YPYIVVVRES PGASRVIEHR FVGLFTVAAM
     NANALEIPLI SRRVEEALAM AHRDPSHPGQ LLRDIIQTIP RPELFALSSK QLLEMALAVV
     DLGSRRRTLL FLRADHLAHF VSCLVYLPRD RYTTAVRLEM QDILVRELGG AGIDYSARVS
     ESPWAVVHFT VRLPEGTAAD SVDTSLENES RIQDLLTEAT RNWGDRMISA AAAASISPAA
     LEHYAHAFPE DYKQAFAPQD AIADISLIEA LQDDSVKLVL ADTAEDRVWK LTWYLGGHSA
     SLSELLPMLQ SMGVVVLEER PFTLRRTDGL PVWIYQFKIS PHPSIPHAPD AEAQRDTAQR
     FADAVTAIWH GRVEIDRFNE LVMRAGLTWQ QVVVLRAYAK YLRQAGFPYS QSHIESVLNE
     NPHTTRSLID LFEALFDPSQ ETDGRRDAQG AAAAVAADID ALVSLDTDRV LRAFANLIEA
     TLRTNYFVAR PDSARARNVL AFKLNPLVIK ELPLPRPKFE IFVYSPRVEG VHLRFGFVAR
     GGLRWSDRRE DFRTEILGLV KAQAVKNAVI VPVGAKGGFV VKRPPTLTGD AAADREATRA
     EGVECYRLFI SGLLDVTDNV DKATGAVVTP PEVVRRDGED AYLVVAADKG TATFSDIANE
     VAKSYGFWLG DAFASGGSIG YDHKAMGITA KGAWESVKRH FREMGVDTQT QDFTVVGIGD
     MSGDVFGNGM LLSKHIRLVA AFDHRDIFLD PNPDAGRSWD ERKRLFDLPR SSWADYDKSL
     ISEGGGVYSR QQKSIPISPQ VRTALGLDAD VEELTPPALI KAILKAPVDL LWNGGIGTYI
     KAETEADADV GDRANDQIRV CGNQVRAKVI GEGGNLGVTA LGRIEFDLAG GRINTDALDN
     SAGVDCSDHE VNIKILIDSA VTAGKVTPEE RTELLLSMTD EVGELVLADN RDQNDLMGTS
     RANAASLLSV HARMIKDLVD NRGLNRELEA LPSEKEIRRR ADAGIGLTSP ELATLMAHVK
     LALKDDVLAS DLPDQEVFAS RLPYYFPTRL REELHGEIRS HQLRREIITT MLVNDLVDTA
     GISYAYRITE DVGVGPVDAV RSYVAINAIF GIGDVWRRIR AAGDAGVPTS VTDRMTLDLR
     RLVDRAGRWL LNYRPQPLAV GAEINRFGAK VAALTPRMSE WLRGDDKAIV SKEAGDFASH
     GVPEDLAYHI ATGLYQYSLL DVIDIADIVD REPDEVADTY FALMDHLGAD ALLTAVSRLS
     RDDRWHSLAR LAIRDDIYGS LRALCFDVLA VGEPDENGEE KIAEWETTNS SRVTRARRTL
     TEIYKDGEQD LATLSVAARQ IRSMTRTSGT GTTG