DHE4_SYNY3
ID DHE4_SYNY3 Reviewed; 428 AA.
AC P54386;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=NADP-specific glutamate dehydrogenase;
DE Short=NADP-GDH;
DE EC=1.4.1.4;
GN Name=gdhA; OrderedLocusNames=slr0710;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7787182; DOI=10.1007/bf00042048;
RA Chavez S., Reyes J.C., Chauvat F., Florencio F.J., Candau P.;
RT "The NADP-glutamate dehydrogenase of the cyanobacterium Synechocystis 6803:
RT cloning, transcriptional analysis and disruption of the gdhA gene.";
RL Plant Mol. Biol. 28:173-188(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Catalyzes the reversible oxidative deamination of glutamate
CC to alpha-ketoglutarate and ammonia. {ECO:0000250}.
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: Homohexamer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; X77454; CAA54601.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA10756.1; -; Genomic_DNA.
DR PIR; S77064; S77064.
DR AlphaFoldDB; P54386; -.
DR SMR; P54386; -.
DR STRING; 1148.1006603; -.
DR PaxDb; P54386; -.
DR EnsemblBacteria; BAA10756; BAA10756; BAA10756.
DR KEGG; syn:slr0710; -.
DR eggNOG; COG0334; Bacteria.
DR InParanoid; P54386; -.
DR OMA; PCFAAFP; -.
DR PhylomeDB; P54386; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; ISS:UniProtKB.
DR GO; GO:0006537; P:glutamate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR CDD; cd01076; NAD_bind_1_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 3: Inferred from homology;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..428
FT /note="NADP-specific glutamate dehydrogenase"
FT /id="PRO_0000182777"
FT ACT_SITE 104
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 144
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 428 AA; 47313 MW; F966273E8D5AD04E CRC64;
MAGSLFADAS KRLEKALKYV AISDDAGERL KYPKTSLSVS IPVRMDDGSL KIFPGYRVRY
DDTRGPGKGG VRYHPNVTMD EVQSLAFWMT FKCALLNLPF GGAKGGITLN PKELSRAELE
RLSRGYIEAI ADFIGPDIDI LAPDVYTNEM MMGWMMDQYS IIRRKISPAV VTGKPVTMGG
SQGRNTATGT GAFYIMQGML PKFDQYPENT TVAVQGFGNA GMVVAECLYQ DGYKVVAISD
SQGGIYNEQG IDIPAVIDYK QRHRTLAGMY CDQAICDLGE NQQISNAELL ALDVDVLIPA
ALENQITRDN ADQVRARYIF EVANGPTTTA ADDILASKGI YVFPDILVNA GGVTVSYFEW
VQNRSGLYWS AKEVNDRLKE KMVEEAEHVW NITQELDVNV RTAAYIHALN RLSEAMDAKG
TRDYYQDS
