ID A0A364RIV9_9BACT Unreviewed; 366 AA.
AC A0A364RIV9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Leucine dehydrogenase {ECO:0000313|EMBL:RAU84178.1};
GN ORFNames=DP923_03805 {ECO:0000313|EMBL:RAU84178.1};
OS Pontibacter arcticus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=2080288 {ECO:0000313|EMBL:RAU84178.1, ECO:0000313|Proteomes:UP000251692};
RN [1] {ECO:0000313|EMBL:RAU84178.1, ECO:0000313|Proteomes:UP000251692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2b14 {ECO:0000313|EMBL:RAU84178.1,
RC ECO:0000313|Proteomes:UP000251692};
RA Liu Z.-W.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RAU84178.1, ECO:0000313|Proteomes:UP000251692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2b14 {ECO:0000313|EMBL:RAU84178.1,
RC ECO:0000313|Proteomes:UP000251692};
RA Du Z.-J.;
RT "Pontibacter sp. 2b14 genomic sequence and assembly.";
RL Submitted (JUL-2018) 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:RAU84178.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QMDV01000001; RAU84178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364RIV9; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000251692; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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 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; 2.
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:UP000251692}.
FT DOMAIN 156..364
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 92
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 192..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 366 AA; 40083 MW; E3AF050CE856F91A CRC64;
MVEIKEVELK KDKSIFGQIS EYNHEKVVFC HDQETGLKAI IGIHNTVLGP ALGGTRMWSY
ASDAEALEDV LRLSRGMTYK AAISGLNLGG GKAVIIGDAK KDKNEALLRR FGRFVKNLNG
AYITAEDVGM TTKDMEYIRM ETEHVSGLPE SMGGSGDPSP VTAYGTYMGM KAAAKKAYGS
DSLEGKKISV QGVGHVGGYL VELLAKENAE IFITDIYEDR LREISTKYGA KTVTMDEIYD
LDVDIYSPCA LGGTINNDTI NRLKCQVIAG CANNQLRDET VHGPALIERG IVYAPDFLIN
AGGLINVYSE LQGYNRESAY AQTERIYGYT LDIFELAEKE GIYTQLAATK MAEQRIQSIG
KVKSTF
//
