ID Q7YZU9_SPIBA Unreviewed; 446 AA.
AC Q7YZU9;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=glutamate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012907};
DE EC=1.4.1.4 {ECO:0000256|ARBA:ARBA00012907};
DE Flags: Fragment;
GN Name=gdh {ECO:0000313|EMBL:AAP83851.1};
OS Spironucleus barkhanus.
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Hexamitinae;
OC Spironucleus.
OX NCBI_TaxID=103874 {ECO:0000313|EMBL:AAP83851.1};
RN [1] {ECO:0000313|EMBL:AAP83851.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 50380 {ECO:0000313|EMBL:AAP83851.1};
RX PubMed=12820901; DOI=10.1186/1471-2148-3-14;
RA Andersson J.O., Roger A.J.;
RT "Evolution of glutamate dehydrogenase genes: evidence for lateral gene
RT transfer within and between prokaryotes and eukaryotes.";
RL BMC Evol. Biol. 3:14-14(2003).
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|RuleBase:RU004417}.
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DR EMBL; AF533884; AAP83851.1; -; mRNA.
DR AlphaFoldDB; Q7YZU9; -.
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; IPR033524; Glu/Leu/Phe/Val_DH_AS.
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.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 2: Evidence at transcript level;
KW NAD {ECO:0000256|PIRSR:PIRSR000185-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417}.
FT DOMAIN 198..444
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 122
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 236
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 162
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAP83851.1"
SQ SEQUENCE 446 AA; 49309 MW; AEB43D2A1762DB80 CRC64;
GTRQDLKNVL QQRDAHNIEF CQAVNEVIDS LTVVFEENPK YISVFEQLLE PERVIMFRVP
WTDDKGEVNI NRGYRVQYNS ALGPYKGGLR FHPSVNISVL KFLGFEQILK NSLTTLPMGG
GKGGSDFDPK GKSNGEVMRF CQSFMTELSR HIGQFTDVPA GDIGVGGREI GYMFGQYKRI
QNQFTGILTG KAYSWGGSLI RPEATGYGAV YYLNEMMLDN GDDIKGKRVL LSGAGNVAQF
ATEKLLHYGA IPLSLSDSNG TIIEPNGFTA EQLKMVMDLK NIKRGRLSEY TSMSSTAKYY
EGQRPWAVYE GKVDVIMPCA TQNEVNGTEA ERVIKLGLRY VSEGANMPSN DDAIHAYHSS
KVFYGPAKAS NAGGVATSGL EMTQNSNRLQ WSAEKVDAEL HAIMKKIFQQ CKQTAEKYNK
KGNYQFGANV AGFLKVADSM IDQGCV
//
