ID   DHE2_PORGI              Reviewed;         445 AA.
AC   P0C934; Q03578;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=PG_1232;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-29.
RX   PubMed=8392971; DOI=10.1128/iai.61.8.3294-3303.1993;
RA   Joe A., Yamamoto A., McBride B.C.;
RT   "Characterization of recombinant and native forms of a cell surface antigen
RT   of Porphyromonas (Bacteroides) gingivalis.";
RL   Infect. Immun. 61:3294-3303(1993).
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; AE015924; AAQ66318.1; -; Genomic_DNA.
DR   RefSeq; WP_010956255.1; NC_002950.2.
DR   AlphaFoldDB; P0C934; -.
DR   SMR; P0C934; -.
DR   STRING; 242619.PG_1232; -.
DR   PRIDE; P0C934; -.
DR   EnsemblBacteria; AAQ66318; AAQ66318; PG_1232.
DR   GeneID; 29256557; -.
DR   KEGG; pgi:PG_1232; -.
DR   eggNOG; COG0334; Bacteria.
DR   HOGENOM; CLU_025763_2_1_10; -.
DR   OMA; PCFAAFP; -.
DR   OrthoDB; 1184827at2; -.
DR   Proteomes; UP000000588; 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   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..445
FT                   /note="NAD-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182740"
FT   ACT_SITE        124
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
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