ID K9U171_CHRTP Unreviewed; 350 AA.
AC K9U171;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:AFY88585.1};
DE EC=1.4.1.9 {ECO:0000313|EMBL:AFY88585.1};
GN ORFNames=Chro_3118 {ECO:0000313|EMBL:AFY88585.1};
OS Chroococcidiopsis thermalis (strain PCC 7203).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Chroococcidiopsidales;
OC Chroococcidiopsidaceae; Chroococcidiopsis.
OX NCBI_TaxID=251229 {ECO:0000313|EMBL:AFY88585.1, ECO:0000313|Proteomes:UP000010384};
RN [1] {ECO:0000313|EMBL:AFY88585.1, ECO:0000313|Proteomes:UP000010384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7203 {ECO:0000313|EMBL:AFY88585.1,
RC ECO:0000313|Proteomes:UP000010384};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Chroococcidiopsis thermalis PCC 7203.";
RL Submitted (JUN-2012) 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}.
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DR EMBL; CP003597; AFY88585.1; -; Genomic_DNA.
DR RefSeq; WP_015155131.1; NC_019695.1.
DR AlphaFoldDB; K9U171; -.
DR STRING; 251229.Chro_3118; -.
DR KEGG; cthe:Chro_3118; -.
DR PATRIC; fig|251229.3.peg.3646; -.
DR eggNOG; COG0334; Bacteria.
DR HOGENOM; CLU_025763_0_0_3; -.
DR InParanoid; K9U171; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000010384; Chromosome.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR GO; GO:0050049; F:leucine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR InterPro; IPR016211; Glu/Phe/Leu/Val/Trp_DH_bac/arc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; NF035922; Trp_DH_ScyB; 1.
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 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.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000188-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000188-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417};
KW Reference proteome {ECO:0000313|Proteomes:UP000010384}.
FT DOMAIN 140..348
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 176..181
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 350 AA; 38552 MW; 07DEE46167F34915 CRC64;
MKLFETVKEM GHEQVLFFQD KELNFKAIIA LHDTSLGRAM GATRLFPYAS EEDALQDVLR
LSRGMTYKAA CANIPVGGGK AVIIANPDQK TDKMLRAYGR FVDSLQGRFI TGQDVNICPE
DVQEMRRETR YVVGLTGKAG GPAPATALGV FLGIQAAVFF QFNKQDLNGL RVAVQGLGNV
GGKLCDYLHR RGVKLFVTDL NHNRAEEIKQ LYGAKVVEPE DIYSLDVDIF APCAMGAILN
SETIPLIQAS IIAGCANNQL QDENIHSAML KSKGIIYCPD YVINSGGLIN VYHELTFSDE
ASYLKQIHSI YDTLLEIFTK SKAENITTQD ASKRLAEERI LKARKLAIAA
//
