ID A0A0A2FRC6_9PORP Unreviewed; 445 AA.
AC A0A0A2FRC6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN Name=gdh {ECO:0000313|EMBL:SQH73169.1};
GN ORFNames=HQ45_07545 {ECO:0000313|EMBL:KGN89376.1}, NCTC12858_01014
GN {ECO:0000313|EMBL:SQH73169.1};
OS Porphyromonas crevioricanis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=393921 {ECO:0000313|EMBL:KGN89376.1, ECO:0000313|Proteomes:UP000030139};
RN [1] {ECO:0000313|EMBL:KGN89376.1, ECO:0000313|Proteomes:UP000030139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-253 OH2125 {ECO:0000313|Proteomes:UP000030139}, and
RC COT-253_OH2125 {ECO:0000313|EMBL:KGN89376.1};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas crevioricanis strain:COT-253_OH2125 Genome sequencing.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SQH73169.1, ECO:0000313|Proteomes:UP000249300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12858 {ECO:0000313|EMBL:SQH73169.1,
RC ECO:0000313|Proteomes:UP000249300};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000185,
CC ECO:0000256|RuleBase:RU004417}.
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DR EMBL; JQJB01000009; KGN89376.1; -; Genomic_DNA.
DR EMBL; LS483447; SQH73169.1; -; Genomic_DNA.
DR RefSeq; WP_023935776.1; NZ_LS483447.1.
DR AlphaFoldDB; A0A0A2FRC6; -.
DR STRING; 393921.HQ45_07545; -.
DR KEGG; pcre:NCTC12858_01014; -.
DR eggNOG; COG0334; Bacteria.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000030139; Unassembled WGS sequence.
DR Proteomes; UP000249300; Chromosome 1.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd05313; NAD_bind_2_Glu_DH; 1.
DR Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 2.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR006095; Glu/Leu/Phe/Val/Trp_DH.
DR InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
DR InterPro; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
DR PANTHER; PTHR43571; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR43571:SF1; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
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; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000185-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000185};
KW Reference proteome {ECO:0000313|Proteomes:UP000249300}.
FT DOMAIN 200..443
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 124
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 164
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 445 AA; 48923 MW; 016A63A1B7215896 CRC64;
MKTSEIMAQL EAKHPGESEF LQAVREVLLS VEEVYNQHPE FEKNGIIERI VEPDRIFTFR
VPWVDDAGKV HVNIGYRVQF NNAIGPYKGG IRFHPSVNLS ILKFLGFEQT FKNALTTLPM
GGGKGGSDFA PKGRSEAEIM RFCQSFMTEL WQNIGPDTDI PAGDIGVGGR EVAYMYGMYK
KLARECTGTM TGKGFEFGGS RLRPESTGFG AVYFVHNMCK AHNIDLKGKT VAISGFGNVA
WGVAMKATEL GAKVVTISGP DGYVYDEEGI NTPEKFACML ELRSSGNDVV SDYVKKFPNA
KFFAGKKPWE QKVDIAMPCA TQNEMNLEDA KMLHKNGVTL VAETSNMGCT AEASEYYVAQ
KMLFAPGKAV NAGGVSCSGL EMTQNAMHLS WSNEEVDKWL HQIMNDIHEQ CVTYGKQGDY
IDYVKGANIA GFMKVAKAMV AQGVC
//
