ID A0A081G445_9GAMM Unreviewed; 348 AA.
AC A0A081G445;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:KEA65550.1};
DE EC=1.4.1.9 {ECO:0000313|EMBL:KEA65550.1};
GN ORFNames=ADIMK_0507 {ECO:0000313|EMBL:KEA65550.1};
OS Marinobacterium lacunae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinobacterium.
OX NCBI_TaxID=1232683 {ECO:0000313|EMBL:KEA65550.1, ECO:0000313|Proteomes:UP000028252};
RN [1] {ECO:0000313|EMBL:KEA65550.1, ECO:0000313|Proteomes:UP000028252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK27 {ECO:0000313|EMBL:KEA65550.1,
RC ECO:0000313|Proteomes:UP000028252};
RA Singh A., Pinnaka A.K.;
RT "Marinobacterium kochiensis sp. nov., isolated from sediment sample
RT collected from Kochi backwaters in Kerala, India.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible oxidative deamination of glutamate
CC to alpha-ketoglutarate and ammonia. {ECO:0000256|ARBA:ARBA00003868}.
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:KEA65550.1}.
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DR EMBL; JMQN01000011; KEA65550.1; -; Genomic_DNA.
DR RefSeq; WP_036183073.1; NZ_JMQN01000011.1.
DR AlphaFoldDB; A0A081G445; -.
DR STRING; 1232683.ADIMK_0507; -.
DR PATRIC; fig|1232683.4.peg.501; -.
DR eggNOG; COG0334; Bacteria.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000028252; Unassembled WGS sequence.
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; 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 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.
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:UP000028252}.
FT DOMAIN 138..345
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 78
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 174..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 348 AA; 37409 MW; F6CBA75B4EAC7DA1 CRC64;
MFRQMEDAGL TDIHIGLDAA TGMRAIVAIH STARGPAIGG CRFIHYANED EALTDVIRLA
RGMSYKAALA DLPHGGGKAV LMRPDRPFDR TALMQAFGRF VDTLGGRYIT AVDSGSEVSD
MDVIARETRW VSCTSAGGDP SPYTAIGVFS GIQAFVRVGL GRPSLDGMRV ALQGLGHVGM
ALAQKFHDAG AHLVVSDLDQ SRLDAAAQQF NARIVAPQEI YSVPCDLFCP CGLGAILNEK
TIPQLRCKIV AGCANNQLAS DDDGERLRER GIFYAPDYII NSGGLIQVAM KHAGASEHAI
LDKIQGVGST LERLLEDAIR LDLPIEKLAD RLAEQRLHAR QTSRHHAA
//
