ID   DHE2_HALED              Reviewed;        1613 AA.
AC   E1V4J5;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000250|UniProtKB:Q9HZE0};
DE            Short=NAD-GDH {ECO:0000250|UniProtKB:Q9HZE0};
DE            EC=1.4.1.2 {ECO:0000269|PubMed:28081159};
DE   AltName: Full=NAD(+)-dependent glutamate dehydrogenase {ECO:0000250|UniProtKB:Q9HZE0};
GN   Name=gdh {ECO:0000303|PubMed:28081159};
GN   OrderedLocusNames=HELO_3049 {ECO:0000312|EMBL:CBV42933.1};
OS   Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS   / 1H9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=768066;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX   PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA   Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA   Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA   Kunte H.J.;
RT   "A blueprint of ectoine metabolism from the genome of the industrial
RT   producer Halomonas elongata DSM 2581(T).";
RL   Environ. Microbiol. 13:1973-1994(2011).
RN   [2]
RP   CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX   PubMed=28081159; DOI=10.1371/journal.pone.0168818;
RA   Kindzierski V., Raschke S., Knabe N., Siedler F., Scheffer B.,
RA   Pflueger-Grau K., Pfeiffer F., Oesterhelt D., Marin-Sanguino A.,
RA   Kunte H.J.;
RT   "Osmoregulation in the halophilic bacterium Halomonas elongata: a case
RT   study for integrative systems biology.";
RL   PLoS ONE 12:E0168818-E0168818(2017).
CC   -!- FUNCTION: Involved in arginine catabolism by converting L-glutamate,
CC       into 2-oxoglutarate, which is then channeled into the tricarboxylic
CC       acid cycle. {ECO:0000250|UniProtKB:Q9HZE0}.
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:28081159};
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; FN869568; CBV42933.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1V4J5; -.
DR   SMR; E1V4J5; -.
DR   STRING; 768066.HELO_3049; -.
DR   EnsemblBacteria; CBV42933; CBV42933; HELO_3049.
DR   KEGG; hel:HELO_3049; -.
DR   eggNOG; COG2902; Bacteria.
DR   HOGENOM; CLU_003404_1_1_6; -.
DR   OMA; RATRWFL; -.
DR   Proteomes; UP000008707; 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   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..1613
FT                   /note="NAD-specific glutamate dehydrogenase"
FT                   /id="PRO_0000439538"
FT   ACT_SITE        849
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1613 AA;  183519 MW;  35A9456FDF3FC7F3 CRC64;
     MLHVAQEEAR LDLLKQLKER LQSRLDKDKA AEVDTFAHLF YAAVPLEDLA DRRLDDLYGA
     TLSVWHFIQQ FDPEAPKVRV LNPDFEEHGW QSTHTFIAVL HEDMPFLVDS VRVELNRRGM
     TVHAIHNAVL AVGRDDEHRL QRVASPEETD APEARESLIA IEVDRHSNPA ELEEIEASLL
     EVLREVRTAV SDFDPMRAQA RAAIEELEAT RPAQVDPADH REAIEFLQWL LQDNFTFLGY
     DEYEVREDQG RQRLDKVQNS ELGVFRLDQP RYRERIRTDL GVEGDHYVPM PQLMSFAKSA
     HHARIHRPTY PDYISIDRYD DQGRVIGERR FLGMFTATVY NESPRNVPIL RRKLQAVMDI
     AGFSPKGHNG KQLLQILEVY PRDDLFQIDI EELAQTALGI LDIRERRRVR LFIREDTFGK
     FYSCLVFVPR DVFSTELRVR LQELLCEELD ATFGDFNTYL SESVLARIQF ILRFNGEKPV
     EYDIKRLEEK LVKLARNWRD DLLNASIEGF GEESANLLMS RFRDAFPASY REDFSARTAV
     YDLQHIGELD EGAPLALSLY RLIEEEGSGV NLKLFHRGAP IPLSDVLPMM ENLGLRVIGE
     RPYEVQASDA SYWIHDFNLE HHTSVEMNLQ EMRGPFIEAF QRIWAGEADN DAFNRLIIGA
     NLDWREVAML RAYARYLKQI RFGMSQDYIA TTLGSHPEIT RELVSLFELR FDPAERPGEG
     DIEECESRIL TLLDEVPSLN DDQLLRRYME LIKATLRTNY YQRTEEGRYK DYLAFKLDPS
     QVSGIPKPCP AYEIFVCSPR VEGVHLRGGK VARGGLRWSD RHEDFRTEVL GLVKAQQVKN
     AVIVPMGAKG GFVCKRMPEG ADREATQKEG IACYQIFIRA LLDVTDNLVG GEVVPPRDVV
     RHDDNDPYLV VAADKGTATF SDIANEISTE YGHWLGDAFA SGGANGYDHK KMAITAKGAW
     ESVKRHFRGL GVNTQEDEFS VVGIGDMAGD VFGNGMLLSD KIRLVGAFNH LHIFVDPTPD
     AAASFAERQR LFDMPRSSWE DYNTELISEG GGIFPRSAKS ITITPQMKKV FGIREDKLSP
     NELIRAMLVS KVDLVWNGGI GTYVKSSEET DAEVGDKAND ALRIDGRELN CRVVGEGGNL
     GLTQRGRMEA AAKGVRVNTD FIDNAGGVNC SDHEVNIKIL IDEVVSRGDL TEKQRNQLLA
     DMTDEVSELV LLDNYRQTQA LDLAELLSRQ GIGPYRRFIS ELEAAGQIDR ELEFLPSDEE
     LLERTQHNQG MTLPELSVLI SYAKSVLKGD LIASDVPDDP TIMRFVERVF PSMLAERYRD
     EMYEHRLKRE IVATQVANDL VDYMGVVFVR RLMDSTGADR ADIARAYVIA RDSFQLPRLW
     EQIEALDNKV PSQVQYSMML DLMRMLRRST RWFLRQRTGM STRDTIDYFA PRLAQLQENI
     GKRLRGEEQE QWSARRQELV KAGVPEALAS TVAAAGSLYA ALGIIQTARQ TDEKPQRVAE
     IFYEVGARLE LPWIIQQVTR LEVRDGWQAK ARDTFRDDID RQQLALTASV LGMDGGPRDS
     AERVDRWLSL HEGMHQRWRH LLEEVGSGSQ GGFPLFAVAV RELVDLAESN SEA