ID   DHE4_CHLSO              Reviewed;         523 AA.
AC   P28998;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-MAY-2023, entry version 96.
DE   RecName: Full=NADP-specific glutamate dehydrogenase;
DE            Short=NADP-GDH;
DE            EC=1.4.1.4;
DE   Flags: Fragment;
OS   Chlorella sorokiniana (Freshwater green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX   NCBI_TaxID=3076;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=1718478; DOI=10.1007/bf00037142;
RA   Cock J.M., Kim K.D., Miller P.W., Hutson R.G., Schmidt R.R.;
RT   "A nuclear gene with many introns encoding ammonium-inducible chloroplastic
RT   NADP-specific glutamate dehydrogenase(s) in Chlorella sorokiniana.";
RL   Plant Mol. Biol. 17:1023-1044(1991).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH +
CC         NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.4;
CC   -!- SUBUNIT: Homo- and heterohexamer of alpha and beta subunits. Both
CC       subunits are encoded by the same gene.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- INDUCTION: By ammonium.
CC   -!- PTM: The N-termini of the alpha and the beta chains are blocked.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000305}.
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DR   EMBL; X58832; CAA41636.1; -; mRNA.
DR   EMBL; X58831; CAA41635.1; -; Genomic_DNA.
DR   PIR; S17949; S17949.
DR   AlphaFoldDB; P28998; -.
DR   SMR; P28998; -.
DR   BRENDA; 1.4.1.4; 1334.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
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; IPR033524; Glu/Leu/Phe/Val_DH_AS.
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   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.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; NADP; Oxidoreductase; Plastid.
FT   CHAIN           <1..523
FT                   /note="NADP-specific glutamate dehydrogenase"
FT                   /id="PRO_0000182782"
FT   REGION          26..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT   CONFLICT        220..221
FT                   /note="FC -> LW (in Ref. 1; CAA41635)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   523 AA;  57530 MW;  A35FE730E5FEF974 CRC64;
     CRPPSSPSLS WPPGLRSPAL PRAVACARGR SAKRDVAAKR LRSRSPRMDA TTGDFTALQK
     AVKQMATKAG TEGLVHGIKN PELRQLLTEI FMKDPEQQEF MQAVREVAVS LQPVFEKRPE
     LLPIFKQIVE PERVITFRVS WLDDAGNLQV NRGFRVQYSS AIGPYKGGLR FHPSVNLSIM
     KFLAFEQIFK NSLTTLPMGG GKGGSDFDPK GKSDAEVMRF CQSFMTELQR HISYVQDVPA
     GDIGVGAREI GYLFGQYKRI TKNYTGVLTG KGQEYGGSEI RPEATGYGAV LFVENVLKDK
     GESLKGKRCL VSGAGNVAQY CAELLLEKGA IVLSLSDSQG YVYEPNGFTR EQLQAVQDMK
     KKNNSARISE YKSDTAVYVG DRRKPWELDC QVDIAFPCAT QNEIDEHDAE LLIKHGCQYV
     VEGANMPSTN EAIHKYNKAG IIYCPGKAAN AGGVAVSGLE MTQNRMSLNW TREEVRDKLE
     RIMKDIYDSA MGPSREYNVD LAAGANIAGF TKVADAVKAQ GAV
//