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Database: UniProt
Entry: N6XJR9_9RHOO
LinkDB: N6XJR9_9RHOO
Original site: N6XJR9_9RHOO 
ID   N6XJR9_9RHOO            Unreviewed;       349 AA.
AC   N6XJR9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Glu/Leu/Phe/Val dehydrogenase dimerization region {ECO:0000313|EMBL:ENO79635.1};
GN   ORFNames=B447_12964 {ECO:0000313|EMBL:ENO79635.1};
OS   Thauera sp. 27.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=305700 {ECO:0000313|EMBL:ENO79635.1, ECO:0000313|Proteomes:UP000013140};
RN   [1] {ECO:0000313|EMBL:ENO79635.1, ECO:0000313|Proteomes:UP000013140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=27 {ECO:0000313|EMBL:ENO79635.1,
RC   ECO:0000313|Proteomes:UP000013140};
RA   Liu B., Shapleigh J.P., Frostegard A.H.;
RT   "Draft Genome Sequences of 6 Strains from Genus Thauera.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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:ENO79635.1}.
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DR   EMBL; AMXB01000022; ENO79635.1; -; Genomic_DNA.
DR   RefSeq; WP_002928627.1; NZ_AMXB01000022.1.
DR   AlphaFoldDB; N6XJR9; -.
DR   SMR; N6XJR9; -.
DR   eggNOG; COG0334; Bacteria.
DR   Proteomes; UP000013140; Unassembled WGS sequence.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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; IPR033524; Glu/Leu/Phe/Val_DH_AS.
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; 2.
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.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000188-2};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000188-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004417};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013140}.
FT   DOMAIN          148..349
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   ACT_SITE        80
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT   BINDING         184..189
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ   SEQUENCE   349 AA;  37646 MW;  368E86E77A47F6E1 CRC64;
     MAVFSLSDFA DHEQVVFVSD DKSGLKAIIA VHNSNLGPAL GGCRMWPYAS EEEAIRDVLR
     LSRGMTYKSA MANLKLGGGK SVIIGNPRTQ KTPELLAAFA RALEQLNGRY IAAEDSGTSV
     ADMKYMTQFT QHVAGIHDKP SDEGTRSGDP SPATAYGTFI GIKAAVKEKL GRDSLEGLRV
     AVQGVGNVGF DLARQLKAAG AQLWVTDIHR EPLLQAGKEL GATVVAPDEI FGLDVDVFAP
     CALGAILNDS TIPQLKAKVV AGASNNQLAE PRHGVELMKR GILYAPDYVI NAGGIIDVYH
     ERIGFDRAAL LKHIEGIHDN LMEVFERARK EERPTGEVAD AIAEERFKR
//
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