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Database: UniProt
Entry: A0A0F2SHX1_9FIRM
LinkDB: A0A0F2SHX1_9FIRM
Original site: A0A0F2SHX1_9FIRM 
ID   A0A0F2SHX1_9FIRM        Unreviewed;       358 AA.
AC   A0A0F2SHX1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:KJS49831.1};
GN   ORFNames=VR66_06460 {ECO:0000313|EMBL:KJS49831.1};
OS   Peptococcaceae bacterium BRH_c23.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1629714 {ECO:0000313|EMBL:KJS49831.1, ECO:0000313|Proteomes:UP000033503};
RN   [1] {ECO:0000313|EMBL:KJS49831.1, ECO:0000313|Proteomes:UP000033503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c23 {ECO:0000313|EMBL:KJS49831.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) 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:KJS49831.1}.
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DR   EMBL; LADV01000072; KJS49831.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2SHX1; -.
DR   PATRIC; fig|1629714.3.peg.4471; -.
DR   Proteomes; UP000033503; 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: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; 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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000188-2};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000188-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004417}.
FT   DOMAIN          144..351
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         180..185
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ   SEQUENCE   358 AA;  39427 MW;  2A1B6857ED7BFE69 CRC64;
     MEIFEYLQKY DYEQLVICQD QTSGLKAIIC IHDTTLGPAL GGTRMWNYAS EEEAIFDALR
     LARGMTYKNA AAGLNLGGGK TVIIGDSHTQ KSEELFRAFG RYVQSLNGRY ITAEDVGTTV
     QDMDWVHLET DFVTGVSSSY GASGDPSPMT ARGVWRGMKA AAMEAYGSDS LTGKTIAIQG
     LGHVGYYLAK HLHEEGAKLI VTDIQDDLIK RVINEMGATA VRPAEIFGVK ADIFAPCAMG
     AVVNDETIPQ FKFSIIAGAA NNVLKEEHHG DKLHELGILY APDYVINCGG VINVADELEG
     YNYERALKKV EMVYDNVAKV LEIAKEYKIP TYIAADRMAE QRIERIGRIR SNYLQTSQ
//
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