ID C6XXL3_PEDHD Unreviewed; 408 AA.
AC C6XXL3;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Glu/Leu/Phe/Val dehydrogenase {ECO:0000313|EMBL:ACU02267.1};
GN OrderedLocusNames=Phep_0041 {ECO:0000313|EMBL:ACU02267.1};
OS Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457
OS / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=485917 {ECO:0000313|EMBL:ACU02267.1, ECO:0000313|Proteomes:UP000000852};
RN [1] {ECO:0000313|EMBL:ACU02267.1, ECO:0000313|Proteomes:UP000000852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 /
RC NCIMB 9290 / NRRL B-14731 / HIM 762-3
RC {ECO:0000313|Proteomes:UP000000852};
RX PubMed=21304637; DOI=10.4056/sigs.22138;
RA Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A.,
RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.C., Saunders E., Chertkov O.,
RA Brettin T., Goker M., Rohde M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Pedobacter heparinus type strain (HIM 762-
RT 3).";
RL Stand. Genomic Sci. 1:54-62(2009).
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382}.
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DR EMBL; CP001681; ACU02267.1; -; Genomic_DNA.
DR RefSeq; WP_012780220.1; NZ_AQGK01000003.1.
DR AlphaFoldDB; C6XXL3; -.
DR STRING; 485917.Phep_0041; -.
DR KEGG; phe:Phep_0041; -.
DR eggNOG; COG0334; Bacteria.
DR HOGENOM; CLU_025763_7_0_10; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000000852; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000852}.
FT DOMAIN 181..408
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 408 AA; 45325 MW; C13BBC072BAF228B CRC64;
MKELLKKFEE KRPEIVFEWK DKDSEAEGWV VINSLRGGAA GGGTRMRKGL DKREVESLAK
TMEVKFTVSG PPIGGAKSGI NFDPADPRKK EVLERWYKAV MPLLKNYYGT GGDLNIDEIH
EVIPITENYG LWHPQEGVIN GHYQARENER IHQIGQLRYG VSKVLEDLNY TPDIKRKYKV
ADMITGYGVA ASIGHFYSIW GGKLSGKRAV IQGWGNVAAA AGYYLTQNGV KIVGIIDRVG
GLICKDGFTQ EEVISLFNNR TGNTLVSPDL IPFELASKEI WDIGAEIFVP AAASRLVQQN
EVDQLIHGGL EVIACGANVP FADKEIFFGS IMEHADKHVA VIPDFISNCG MARVFAYLMQ
RNVEMSDDAI FTDASQVIYK ALKAVHEESR EKKELSKTAF EIALKQLV
//
