ID   A8UDU7_9FLAO            Unreviewed;       361 AA.
AC   A8UDU7;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Glutamate dehydrogenase (NAD(P)+) {ECO:0000313|EMBL:EDP72206.1};
GN   ORFNames=FBALC1_13932 {ECO:0000313|EMBL:EDP72206.1};
OS   Flavobacteriales bacterium ALC-1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX   NCBI_TaxID=391603 {ECO:0000313|EMBL:EDP72206.1, ECO:0000313|Proteomes:UP000003630};
RN   [1] {ECO:0000313|EMBL:EDP72206.1, ECO:0000313|Proteomes:UP000003630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALC-1 {ECO:0000313|EMBL:EDP72206.1,
RC   ECO:0000313|Proteomes:UP000003630};
RA   Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (OCT-2007) 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:EDP72206.1}.
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DR   EMBL; ABHI01000001; EDP72206.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8UDU7; -.
DR   STRING; 391603.FBALC1_13932; -.
DR   eggNOG; COG0334; Bacteria.
DR   Proteomes; UP000003630; 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; 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; 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   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:UP000003630}.
FT   DOMAIN          182..359
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
SQ   SEQUENCE   361 AA;  39986 MW;  43AD4C4AE3AFD234 CRC64;
     MIKELLQKYE NKTPEIVFHW NDSETDAEGW TVINSLRGGA AGGGTRMRKG LDRNEVLSLA
     KTMEVKFTVS GPKIGGAKSG INFDPHDPRK KGVLERWYSA VSPLLKSYYG TGGDLNVDEI
     HEVIPITEES GVWHPQEGVF EGHFKPTQAD KINRIGQLRQ GVIKVIENTK YSPDVSRKYT
     VADMITGYGV AIAAKHFYDL NEDSIKGKRV VVQGFGNVGA AAAFYFAQMG AKVVGIIDRV
     GGLINTEGFS FKEITELYLN KNGNTLVSDN LIPFNEINEK IWSLQTEVFA PCAASRLITQ
     SQIDQMISTG LEVITCGANV PFADKEIFFG PIMEHTDQKV SLIPDFFQIV VWQEFCVFYG
     A
//