ID   C0D891_9FIRM            Unreviewed;       376 AA.
AC   C0D891;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Glutamate/leucine/phenylalanine/valine dehydrogenase {ECO:0000313|EMBL:EEG52478.1};
GN   ORFNames=CLOSTASPAR_05489 {ECO:0000313|EMBL:EEG52478.1};
OS   [Clostridium] asparagiforme DSM 15981.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Enterocloster.
OX   NCBI_TaxID=518636 {ECO:0000313|EMBL:EEG52478.1, ECO:0000313|Proteomes:UP000004756};
RN   [1] {ECO:0000313|EMBL:EEG52478.1, ECO:0000313|Proteomes:UP000004756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG52478.1,
RC   ECO:0000313|Proteomes:UP000004756};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEG52478.1, ECO:0000313|Proteomes:UP000004756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG52478.1,
RC   ECO:0000313|Proteomes:UP000004756};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Clostridium asparagiforme (DSM 15981).";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382}.
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:EEG52478.1}.
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DR   EMBL; ACCJ01000448; EEG52478.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0D891; -.
DR   HOGENOM; CLU_025763_7_0_9; -.
DR   Proteomes; UP000004756; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; 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; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11606:SF13; GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
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}.
FT   DOMAIN          152..363
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
SQ   SEQUENCE   376 AA;  40971 MW;  4BC8B776A06628B7 CRC64;
     MCIEWNDTES EAVGWLVIHN FVNGYTGGGI RMHPAVTREE VLRLAECMAY KYKAGESRFC
     GGCKGGIAYD SRRPDAGEVL RRYIIAMMPY IRTGVSLGGD YGTRYGDILK IFSEFGLDMP
     MTKSMRADPK IMENMEAYNR LLDETVYGRP LNDVIAGYGV ACSADEAFAA LAPGRKADVV
     IQGMGRVAFG CASRLAELGH RIVGMADSQV FVYCAQGLDA EALYRMKRES RVPDRDGLPE
     GWETYPTEAC VAAECDVLIP AALANTVNGD NAASVKAGLV VEAANIAVSP EADEILKERG
     VRLICDFTAN LSEAWLYDAV FFGAVTPELS SVLAGAEALC RRNAAKQMRC ALEDGIYARE
     SARELFEPDV QDLPEI
//