ID A0A1U8AV12_NELNU Unreviewed; 637 AA.
AC A0A1U8AV12;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=glutamate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012907};
DE EC=1.4.1.4 {ECO:0000256|ARBA:ARBA00012907};
GN Name=LOC104604421 {ECO:0000313|RefSeq:XP_010267044.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010267044.1};
RN [1] {ECO:0000313|RefSeq:XP_010267044.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_010267044.1; XM_010268742.2.
DR AlphaFoldDB; A0A1U8AV12; -.
DR GeneID; 104604421; -.
DR OrthoDB; 45283at2759; -.
DR Proteomes; UP000189703; Unplaced.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR036291; NAD(P)-bd_dom_sf.
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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417};
KW Reference proteome {ECO:0000313|Proteomes:UP000189703}.
FT DOMAIN 389..635
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 38..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 71623 MW; 3B6574237D682FF8 CRC64;
MLVSRRVVGM NSAMDDINLL QQRHHLVVRE IGEEIDLEIG PGDDDPSFAN TPLMGVPPRE
PSAEEQEEHK QLLMAAQNQN EEQEVPKTQP TKKKKKVVKR WREEWADTYK WAYVDVKEGT
ARIFCSVCRE YGRKHRRNPY GNEGSRNMQM SALEEHNNSL LHKEALRLQM ASKDKIITIA
DKPIYVKALM SKTAGSIVEA VLRRDPHEVE FIQSVQEAVH SLERVIAKNT HYIHILERLL
EPERMIVFRV PWVDDRGETH VNRGFRVQFS QVLGPCRGGL RYHPSMNLST AKFLGFEQTL
KNALSPYKLG GAGGGSDFDP KGKSENEIMR FCQSYMDELY RYLGPDQDLP AEDMGVGPRE
MGYLFGQYRR LAGHFQGSFT GPRIFWSGSS LRTEATGYGL VFFAQIMLAE MNKELKGLRC
VVSGCGKIAM HVLEKLLAYG AVPITVSDSK GYLVDEDGFD YVKISLLRDI KAHQRSLRDY
SKTYARSKYY DEAKPWNERC DVAFPCAAQN EIDQSDAVNL VNSGCRILIE GSNMPCTPEA
IDVLRKANVL VAPAKAAGAG GVAAGELELN HECNLMHWSP EDFETKLQDV MKQTYQKAIK
AATDFGYQKE SPEALVHGAT IAAFLTLAQG MTDQGCV
//
