ID Q063G8_9SYNE Unreviewed; 350 AA.
AC Q063G8;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Glutamate dehydrogenase/leucine dehydrogenase-like protein {ECO:0000313|EMBL:EAU70934.1};
GN ORFNames=BL107_05374 {ECO:0000313|EMBL:EAU70934.1};
OS Synechococcus sp. BL107.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=313625 {ECO:0000313|EMBL:EAU70934.1, ECO:0000313|Proteomes:UP000004390};
RN [1] {ECO:0000313|EMBL:EAU70934.1, ECO:0000313|Proteomes:UP000004390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL107 {ECO:0000313|EMBL:EAU70934.1,
RC ECO:0000313|Proteomes:UP000004390};
RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (OCT-2006) 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:EAU70934.1}.
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DR EMBL; AATZ01000002; EAU70934.1; -; Genomic_DNA.
DR RefSeq; WP_009788302.1; NZ_DS022298.1.
DR AlphaFoldDB; Q063G8; -.
DR STRING; 313625.BL107_05374; -.
DR eggNOG; COG0334; Bacteria.
DR HOGENOM; CLU_067820_0_0_3; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000004390; 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 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 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}.
FT DOMAIN 136..319
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 350 AA; 36559 MW; E553F1B0893200C8 CRC64;
MANATKPEPT VSVLAQHVSA HLSVFVVAEN TDSKRPANGG LRLLNYPSDE ACIADGQRLA
GLMTHKHDLY GTGFAGGKIV ARAQEPAAVK DELISVTAGL LESLDGSMIT GCDLNTSLED
MERLMSLTPH VLAAVGSPVD ASAATAHGTL GAVEAVLSSD LKDAPPGRAL VHGCGAVGGT
VAKTLVDQGW TVFTVDLNRE RAGLAGATPL PPSCPWWEVK VDLMLPCSIS GLINSEIAEG
MRTKAVVPAA NAPFQNPQLA DELRQRGIPV LPDPLVNAGA VIADSIERFS PQAWKGAGAE
DVYAFVRGEV RRRATEYLSQ REQGLSVGDA LTEVAADTTD PIGLSFKDTP
//
