ID M0LSP1_9EURY Unreviewed; 353 AA.
AC M0LSP1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Glu/Leu/Phe/Val dehydrogenase {ECO:0000313|EMBL:EMA35115.1};
GN ORFNames=C446_13194 {ECO:0000313|EMBL:EMA35115.1};
OS Halobiforma nitratireducens JCM 10879.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halobiforma.
OX NCBI_TaxID=1227454 {ECO:0000313|EMBL:EMA35115.1, ECO:0000313|Proteomes:UP000011607};
RN [1] {ECO:0000313|EMBL:EMA35115.1, ECO:0000313|Proteomes:UP000011607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10879 {ECO:0000313|EMBL:EMA35115.1,
RC ECO:0000313|Proteomes:UP000011607};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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}.
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:EMA35115.1}.
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DR EMBL; AOMA01000128; EMA35115.1; -; Genomic_DNA.
DR RefSeq; WP_006673544.1; NZ_AOMA01000128.1.
DR AlphaFoldDB; M0LSP1; -.
DR STRING; 1227454.C446_13194; -.
DR PATRIC; fig|1227454.3.peg.2710; -.
DR eggNOG; arCOG01352; Archaea.
DR OrthoDB; 6425at2157; -.
DR Proteomes; UP000011607; Unassembled WGS sequence.
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; cd01075; NAD_bind_Leu_Phe_Val_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; IPR016211; Glu/Phe/Leu/Val/Trp_DH_bac/arc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42722; LEUCINE DEHYDROGENASE; 1.
DR PANTHER; PTHR42722:SF1; VALINE DEHYDROGENASE; 1.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR Pfam; PF02812; ELFV_dehydrog_N; 1.
DR PIRSF; PIRSF000188; Phe_leu_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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417};
KW Reference proteome {ECO:0000313|Proteomes:UP000011607}.
FT DOMAIN 140..347
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 334..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 79
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
SQ SEQUENCE 353 AA; 37615 MW; 40458DADA5450C20 CRC64;
MVFDSVDDRG HEQVSYFTDP ETGLQAIVAI HDTTLGPSLG GTRFYDYDTE DDALEDVLRL
SEAMTYKAAA ADLPLGGGKA VIMGKPDDLK TEDLLEAYGR AVDRLGGRYI TSVDVNTGVE
DMETVRRTTD HVVGTSDGLG NPSPITAHGV FNGIRACVEH VYDTDSFDGL EVVVQGLGKV
GESLTAELAD HGAEVTVSDI DEDHVAAVAD EYGVDTVAPD EVYDASCDVF APCAVGGVIN
DDTIPQLDCD IVAGAANNVL AERRHAEVLR EEGIVYAPDY VINAGGLITV AKEHLGGTRE
EAFDEAAAIG DRLSEMIDRA ERRDTTVLAA AEEYAEERIE DADSTDETAI PAE
//
