ID   A0A0P9ABS4_9RHOB        Unreviewed;       476 AA.
AC   A0A0P9ABS4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   ORFNames=JI58_05725 {ECO:0000313|EMBL:KPU84131.1};
OS   Marinosulfonomonas sp. PRT-SC04.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Marinosulfonomonas.
OX   NCBI_TaxID=1527300 {ECO:0000313|EMBL:KPU84131.1, ECO:0000313|Proteomes:UP000054415};
RN   [1] {ECO:0000313|EMBL:KPU84131.1, ECO:0000313|Proteomes:UP000054415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRT-SC04 {ECO:0000313|EMBL:KPU84131.1};
RA   Leon Zayas R.I., Novotny M., Podell S., Shepard C.M., Berkenpas E.,
RA   Nikolenko S., Pevzner P., Lasken R.S., Bartlett D.H.;
RT   "Microbial Metabolic Properties Below 8,000 Meters Depth Within the Puerto
RT   Rico Trench Inferred From Single Cell Genomes.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPU84131.1}.
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DR   EMBL; JPUR01000175; KPU84131.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P9ABS4; -.
DR   PATRIC; fig|1527300.3.peg.1214; -.
DR   Proteomes; UP000054415; Unassembled WGS sequence.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd01076; NAD_bind_1_Glu_DH; 1.
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; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11606:SF13; GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL; 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:UP000054415}.
FT   DOMAIN          188..475
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        107
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT   BINDING         71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         195
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         234
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   BINDING         364
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT   SITE            149
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ   SEQUENCE   476 AA;  52697 MW;  EAFD73069F30B480 CRC64;
     MSVTNEPSFR ESVDMMFNRA VALMELAPGL EEKIRVVNAT YTVRFGVRLR GEIKTFTGYR
     SVHSEHMEPV KGGIRFAPSV NQDEVEALGA LMTYKCALVE APFGGSKGGL RIDPRDYNEQ
     EMELITRRFA YELIKRDLIN PSQNVPAPDM GTGEREMAWI ADQYARMNTT DINAKACVTG
     KPLHAGGIAG RIEATGRGVQ YALREFFRHP EDIAIAGLDG SLKGKNIIVQ GLGNVGYHAA
     KFLSEEDGAK IVGIIERDGS LYDPEGLDVE AVHNWMGEHG GLAGYSDTHF NEDGAKLLEM
     KCDILIPAAL ESVINLTNAD RIQAPLIIEA ANGPITAGAD EVLRKKGTVI IPDLYANAGG
     VTVSYFEWVK NLSHIRFGRM QRRQEESRHQ LVVDELERLD SSLGDKWSMS PDFKSQYLRG
     ADELELVRSG LDDTMRAAYQ SMREVWHSRD EVEDLRTAAF IVAITRVAKA YTAKGL
//