ID   DHE2_MYCTU              Reviewed;        1624 AA.
AC   O53203; L0T9R1;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=Rv2476c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   INTERACTION WITH GARA.
RC   STRAIN=ATCC 25618 / H37Rv;
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).
RN   [3]
RP   ACTIVITY REGULATION, AND INTERACTION WITH GARA.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=19318624; DOI=10.1126/scisignal.2000212;
RA   Nott T.J., Kelly G., Stach L., Li J., Westcott S., Patel D., Hunt D.M.,
RA   Howell S., Buxton R.S., O'Hare H.M., Smerdon S.J.;
RT   "An intramolecular switch regulates phosphoindependent FHA domain
RT   interactions in Mycobacterium tuberculosis.";
RL   Sci. Signal. 2:RA12-RA12(2009).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Catalyzes the reversible conversion of L-glutamate to 2-
CC       oxoglutarate. {ECO:0000250}.
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   -!- ACTIVITY REGULATION: Activity is inhibited by unphosphorylated GarA.
CC       {ECO:0000269|PubMed:19318624}.
CC   -!- SUBUNIT: Interacts with (unphosphorylated) GarA.
CC       {ECO:0000269|PubMed:19019160, ECO:0000269|PubMed:19318624}.
CC   -!- INTERACTION:
CC       O53203; P9WJA9: garA; NbExp=5; IntAct=EBI-6405569, EBI-6405522;
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP45270.1; -; Genomic_DNA.
DR   PIR; C70867; C70867.
DR   RefSeq; NP_216992.1; NC_000962.3.
DR   RefSeq; WP_003916039.1; NZ_NVQJ01000024.1.
DR   AlphaFoldDB; O53203; -.
DR   SMR; O53203; -.
DR   IntAct; O53203; 1.
DR   STRING; 83332.Rv2476c; -.
DR   PaxDb; O53203; -.
DR   PRIDE; O53203; -.
DR   GeneID; 887437; -.
DR   KEGG; mtu:Rv2476c; -.
DR   TubercuList; Rv2476c; -.
DR   eggNOG; COG2902; Bacteria.
DR   InParanoid; O53203; -.
DR   OMA; RATRWFL; -.
DR   PhylomeDB; O53203; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
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   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..1624
FT                   /note="NAD-specific glutamate dehydrogenase"
FT                   /id="PRO_0000419536"
FT   ACT_SITE        845
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1624 AA;  176900 MW;  B8ED8C54C24CCFAA CRC64;
     MTIDPGAKQD VEAWTTFTAS ADIPDWISKA YIDSYRGPRD DSSEATKAAE ASWLPASLLT
     PAMLGAHYRL GRHRAAGESC VAVYRADDPA GFGPALQVVA EHGGMLMDSV TVLLHRLGIA
     YAAILTPVFD VHRSPTGELL RIEPKAEGTS PHLGEAWMHV ALSPAVDHKG LAEVERLLPK
     VLADVQRVAT DATALIATLS ELAGEVESNA GGRFSAPDRQ DVGELLRWLG DGNFLLLGYQ
     RCRVADGMVY GEGSSGMGVL RGRTGSRPRL TDDDKLLVLA QARVGSYLRY GAYPYAIAVR
     EYVDGSVVEH RFVGLFSVAA MNADVLEIPT ISRRVREALA MAESDPSHPG QLLLDVIQTV
     PRPELFTLSA QRLLTMARAV VDLGSQRQAL LFLRADRLQY FVSCLVYMPR DRYTTAVRMQ
     FEDILVREFG GTRLEFTARV SESPWALMHF MVRLPEVGVA GEGAAAPPVD VSEANRIRIQ
     GLLTEAARTW ADRLIGAAAA AGSVGQADAM HYAAAFSEAY KQAVTPADAI GDIAVITELT
     DDSVKLVFSE RDEQGVAQLT WFLGGRTASL SQLLPMLQSM GVVVLEERPF SVTRPDGLPV
     WIYQFKISPH PTIPLAPTVA ERAATAHRFA EAVTAIWHGR VEIDRFNELV MRAGLTWQQV
     VLLRAYAKYL RQAGFPYSQS YIESVLNEHP ATVRSLVDLF EALFVPVPSG SASNRDAQAA
     AAAVAADIDA LVSLDTDRIL RAFASLVQAT LRTNYFVTRQ GSARCRDVLA LKLNAQLIDE
     LPLPRPRYEI FVYSPRVEGV HLRFGPVARG GLRWSDRRDD FRTEILGLVK AQAVKNAVIV
     PVGAKGGFVV KRPPLPTGDP AADRDATRAE GVACYQLFIS GLLDVTDNVD HATASVNPPP
     EVVRRDGDDA YLVVAADKGT ATFSDIANDV AKSYGFWLGD AFASGGSVGY DHKAMGITAR
     GAWEAVKRHF REIGIDTQTQ DFTVVGIGDM SGDVFGNGML LSKHIRLIAA FDHRHIFLDP
     NPDAAVSWAE RRRMFELPRS SWSDYDRSLI SEGGGVYSRE QKAIPLSAQV RAVLGIDGSV
     DGGAAEMAPP NLIRAILRAP VDLLFNGGIG TYIKAESESD ADVGDRANDP VRVNANQVRA
     KVIGEGGNLG VTALGRVEFD LSGGRINTDA LDNSAGVDCS DHEVNIKILI DSLVSAGTVK
     ADERTQLLES MTDEVAQLVL ADNEDQNDLM GTSRANAASL LPVHAMQIKY LVAERGVNRE
     LEALPSEKEI ARRSEAGIGL TSPELATLMA HVKLGLKEEV LATELPDQDV FASRLPRYFP
     TALRERFTPE IRSHQLRREI VTTMLINDLV DTAGITYAFR IAEDVGVTPI DAVRTYVATD
     AIFGVGHIWR RIRAANLPIA LSDRLTLDTR RLIDRAGRWL LNYRPQPLAV GAEINRFAAM
     VKALTPRMSE WLRGDDKAIV EKTAAEFASQ GVPEDLAYRV STGLYRYSLL DIIDIADIAD
     IDAAEVADTY FALMDRLGTD GLLTAVSQLP RHDRWHSLAR LAIRDDIYGA LRSLCFDVLA
     VGEPGESSEQ KIAEWEHLSA SRVARARRTL DDIRASGQKD LATLSVAARQ IRRMTRTSGR
     GISG