ID   DHE2_PSEAE              Reviewed;        1620 AA.
AC   Q9HZE0; Q7BHF2;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000305};
DE            Short=NAD-GDH {ECO:0000303|PubMed:11133942};
DE            EC=1.4.1.2 {ECO:0000269|PubMed:11133942};
DE   AltName: Full=NAD(+)-dependent glutamate dehydrogenase {ECO:0000303|PubMed:11133942};
GN   Name=gdhB; OrderedLocusNames=PA3068;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION,
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBUNIT, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11133942; DOI=10.1128/jb.183.2.490-499.2001;
RA   Lu C.D., Abdelal A.T.;
RT   "The gdhB gene of Pseudomonas aeruginosa encodes an arginine-inducible
RT   NAD(+)-dependent glutamate dehydrogenase which is subject to allosteric
RT   regulation.";
RL   J. Bacteriol. 183:490-499(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [3]
RP   INDUCTION BY ARGININE.
RX   PubMed=9286980; DOI=10.1128/jb.179.17.5300-5308.1997;
RA   Park S.-M., Lu C.-D., Abdelal A.T.;
RT   "Cloning and characterization of argR, a gene that participates in
RT   regulation of arginine biosynthesis and catabolism in Pseudomonas
RT   aeruginosa PAO1.";
RL   J. Bacteriol. 179:5300-5308(1997).
CC   -!- FUNCTION: Involved in arginine catabolism by converting L-glutamate,
CC       into 2-oxoglutarate, which is then channeled into the tricarboxylic
CC       acid cycle. Can also utilize other amino acids of the glutamate family.
CC       {ECO:0000269|PubMed:11133942}.
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:11133942};
CC   -!- ACTIVITY REGULATION: Activity subject to allosteric control by arginine
CC       and citrate, which function as positive and negative effectors,
CC       respectively. {ECO:0000269|PubMed:11133942}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.13 uM for NAD {ECO:0000269|PubMed:11133942};
CC       pH dependence:
CC         Optimum pH is 8 for amination, and 9 for deamination.
CC         {ECO:0000269|PubMed:11133942};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11133942}.
CC   -!- INDUCTION: Expression induced by arginine in an ArgR-dependent manner
CC       (27-fold). Induced to a much lesser extent by ornithine, glutamate, and
CC       aspartate (1.7- to 5-fold). {ECO:0000269|PubMed:11133942,
CC       ECO:0000269|PubMed:9286980}.
CC   -!- PTM: Contains disulfide bonds (interchain). {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Reduced growth when arginine serve as the sole
CC       source of carbon and nitrogen. {ECO:0000269|PubMed:11133942}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; AF315586; AAG53963.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG06456.1; -; Genomic_DNA.
DR   PIR; E83261; E83261.
DR   RefSeq; NP_251758.1; NC_002516.2.
DR   RefSeq; WP_003103491.1; NZ_QZGE01000009.1.
DR   AlphaFoldDB; Q9HZE0; -.
DR   SMR; Q9HZE0; -.
DR   STRING; 287.DR97_4868; -.
DR   PaxDb; Q9HZE0; -.
DR   PRIDE; Q9HZE0; -.
DR   EnsemblBacteria; AAG06456; AAG06456; PA3068.
DR   GeneID; 878664; -.
DR   KEGG; pae:PA3068; -.
DR   PATRIC; fig|208964.12.peg.3219; -.
DR   PseudoCAP; PA3068; -.
DR   HOGENOM; CLU_003404_1_1_6; -.
DR   InParanoid; Q9HZE0; -.
DR   OMA; RATRWFL; -.
DR   PhylomeDB; Q9HZE0; -.
DR   BioCyc; PAER208964:G1FZ6-3121-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IDA:CACAO.
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   Direct protein sequencing; Disulfide bond; NAD; Oxidoreductase;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11133942"
FT   CHAIN           2..1620
FT                   /note="NAD-specific glutamate dehydrogenase"
FT                   /id="PRO_0000393369"
FT   ACT_SITE        851
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1620 AA;  182638 MW;  1AF2AE56BE3274C3 CRC64;
     MAFFTAASKA DFQHQLQTAL AQHLGDKALP QVTLFAEQFF SLISLDELTQ RRLSDLVGCT
     LSAWRLLERF DRDQPEVRVY NPDYEKHGWQ STHTAVEVLH PDLPFLVDSV RMELNRRGYS
     IHTLQTNVLS VRRSAKGELK EILPKGSQGK DVSQESLMYL EIDRCAHAGE LRALEKAILE
     VLGEVRVTVA DFEPMKAKAR ELLTWLGKAK LKVPAEELKE VRSYLEWLLD NHFTFLGYEE
     FSVADEADGG RMVYDEKSFL GLTRLLRAGL SKDDLHIEDY AVAYLREPVL LSFAKAAHPS
     RVHRPAYPDY VSIRELDGKG RVIRECRFMG LFTSSVYNES VNDIPFIRGK VAEVMRRSGF
     DTKAHLGKEL AQVLEVLPRD DLFQTPVDEL FSTALAIVRI QERNKIRVFL RKDPYGRFCY
     CLAYVPRDVY STETRLKIQQ VLMERLQASD CEFWTFFSES VLARVQFILR VDPKSRIDID
     PARLEEEVIQ ACRSWQDDYS SLVVENLGEA KGTNVLADFP KGFPAGYRER FAPHFAVVDL
     QHLLSLSEQR PLVMSFYQPL AQGEQQLHCK LYHADTPLAL SDVLPILENL GLRVLGEFPY
     RLRHQNGREY WIHDFAFTYA EGLDVDIQQL NEILQDAFVH IVSGDAENDA FNRLVLTANL
     PWRDVALLRA YARYLKQIRL GFDLGYIASA LNAHTDIARE LVRLFKTRFY LARKLTAEDL
     EDKQQKLEQA ILGALDEVQV LNEDRILRRY LDLIKATLRT NFYQPDGNGQ NKSYFSFKFN
     PKAIPELPRP VPKYEIFVYS PRVEGVHLRG GKVARGGLRW SDREEDFRTE VLGLVKAQQV
     KNAVIVPVGA KGGFVPRRLP LGGSRDEIQA EAIACYRIFI SGLLDITDNL KEGEVVPPAN
     VVRHDEDDPY LVVAADKGTA TFSDIANGIA AEYGFWLGDA FASGGSAGYD HKGMGITAKG
     AWVSVQRHFR ERGIDVQKDN ISVIGIGDMA GDVFGNGLLM SDKLQLVAAF NHMHIFIDPN
     PDAASSFVER QRLFNLPRSS WADYDAKLIS AGGGIFLRSA KSIAITPEMK ARFDIQADRL
     APTELIHALL KAPVDLLWNG GIGTYVKSSK ETHADVGDKA NDGLRVDGRE LRAKVVGEGG
     NLGMTQLARV EFGLHGGANN TDFIDNAGGV DCSDHEVNIK ILLNEVVQAG DMTEKQRNAL
     LVKMTDAVGA LVLGNNYKQT QALSLAQRRA RERIAEYKRL MGDLEARGKL DRALEFLPSD
     EELAERISAG QGLTRAELSV LISYSKIDLK ESLLKSLVPD DDYLTRDMET AFPALLAEKF
     GDAMRRHRLK REIVSTQIAN DLVNHMGITF VQRLKESTGM SAANVAGAYV IVRDVFHLPH
     WFRQIENLDY QVPADIQLTL MDELMRLGRR ATRWFLRSRR NELDAARDVA HFGPRIAALG
     LKLNELLEGP TRELWQARYQ TYVDAGVPEL LARMVAGTSH LYTLLPIIEA SDVTGQDTAE
     VAKAYFAVGS ALDLTWYLQQ ITNLPVENNW QALAREAFRD DLDWQQRAIT VSVLQMQDGP
     KEVEARVGLW LEQHLPLVER WRAMLVELRA ASGTDYAMYA VANRELMDLA QSSQHGVCIP