ID   DHE2_PORG3              Reviewed;         445 AA.
AC   B2RKJ1; Q03578;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=NAD-specific glutamate dehydrogenase;
DE            Short=NAD-GDH;
DE            EC=1.4.1.2;
DE   AltName: Full=Surface-associated protein PGAG1;
GN   Name=gdh; OrderedLocusNames=PGN_1367;
OS   Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS   12257 / NCTC 11834 / 2561).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=431947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8132343; DOI=10.1128/iai.62.4.1358-1368.1994;
RA   Joe A., Murray C.S., McBride B.C.;
RT   "Nucleotide sequence of a Porphyromonas gingivalis gene encoding a surface-
RT   associated glutamate dehydrogenase and construction of a glutamate
RT   dehydrogenase-deficient isogenic mutant.";
RL   Infect. Immun. 62:1358-1368(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX   PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA   Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA   Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA   Nakayama K.;
RT   "Determination of the genome sequence of Porphyromonas gingivalis strain
RT   ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT   rearrangements in P. gingivalis.";
RL   DNA Res. 15:215-225(2008).
CC   -!- FUNCTION: Probably involved in degradation rather than biosynthesis of
CC       glutamate.
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   -!- SUBUNIT: Homohexamer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell surface.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; L07290; AAA50985.1; -; Genomic_DNA.
DR   EMBL; AP009380; BAG33886.1; -; Genomic_DNA.
DR   RefSeq; WP_010956255.1; NZ_CP025930.1.
DR   AlphaFoldDB; B2RKJ1; -.
DR   SMR; B2RKJ1; -.
DR   STRING; 431947.PGN_1367; -.
DR   EnsemblBacteria; BAG33886; BAG33886; PGN_1367.
DR   GeneID; 29256557; -.
DR   KEGG; pgn:PGN_1367; -.
DR   eggNOG; COG0334; Bacteria.
DR   HOGENOM; CLU_025763_2_1_10; -.
DR   OMA; PCFAAFP; -.
DR   BioCyc; PGIN431947:G1G2V-1553-MON; -.
DR   Proteomes; UP000008842; Chromosome.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   CDD; cd05313; NAD_bind_2_Glu_DH; 1.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR   InterPro; IPR014362; Glu_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000185; Glu_DH; 1.
DR   PRINTS; PR00082; GLFDHDRGNASE.
DR   SMART; SM00839; ELFV_dehydrog; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..445
FT                   /note="NAD-specific glutamate dehydrogenase"
FT                   /id="PRO_0000370692"
FT   ACT_SITE        124
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   CONFLICT        258
FT                   /note="S -> Y (in Ref. 1; AAA50985)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   445 AA;  49199 MW;  7436A9C2E01C503D CRC64;
     MKTQEIMTML EAKHPGESEF LQAVKEVLLS VEEVYNQHPE FEKNGIIERI VEPDRVFTFR
     VPWVDDQGKV QVNIGYRVQF NNAIGPYKGG IRFHPSVNLS ILKFLGFEQM FKNALTTLPM
     GGGKGGADFS PKGKSEAEIM RFCQSFMTEL WRNIGPDTDI PAGDIGVGGR EVGYMFGMYK
     KLAREHTGTL TGKGFEFGGS RLRPESTGFG AVYFVQNMCK QNGVDYKGKT LAISGFGNVA
     WGVAQKATEL GIKVVTISGP DGYVYDPDGI NTPEKFRCML DLRDSGNDVV SDYVKRFPNA
     QFFPGKKPWE QKVDFAMPCA TQNEMNLEDA KTLHKNGVTL VAETSNMGCT AEASEYYVAN
     KMLFAPGKAV NAGGVSCSGL EMTQNAMHLV WTNEEVDKWL HQIMQDIHEQ CVTYGKDGNY
     IDYVKGANIA GFMKVAKAMV AQGVC