ID H3ZAQ0_9ALTE Unreviewed; 347 AA.
AC H3ZAQ0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Glu/Leu/Phe/Val dehydrogenase, dimerization region {ECO:0000313|EMBL:EHR42014.1};
GN ORFNames=AJE_02016 {ECO:0000313|EMBL:EHR42014.1};
OS Alishewanella jeotgali KCTC 22429.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alishewanella.
OX NCBI_TaxID=1129374 {ECO:0000313|EMBL:EHR42014.1, ECO:0000313|Proteomes:UP000012046};
RN [1] {ECO:0000313|EMBL:EHR42014.1, ECO:0000313|Proteomes:UP000012046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22429 {ECO:0000313|EMBL:EHR42014.1,
RC ECO:0000313|Proteomes:UP000012046};
RX PubMed=22461542; DOI=10.1128/JB.00153-12;
RA Jung J., Chun J., Park W.;
RT "Genome Sequence of Extracellular-Protease-Producing Alishewanella jeotgali
RT Isolated from Traditional Korean Fermented Seafood.";
RL J. Bacteriol. 194:2097-2097(2012).
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:EHR42014.1}.
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; AHTH01000005; EHR42014.1; -; Genomic_DNA.
DR RefSeq; WP_008949430.1; NZ_AHTH01000005.1.
DR AlphaFoldDB; H3ZAQ0; -.
DR STRING; 1129374.AJE_02016; -.
DR PATRIC; fig|1129374.4.peg.406; -.
DR eggNOG; COG0334; Bacteria.
DR Proteomes; UP000012046; 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}.
FT DOMAIN 141..345
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 177..182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 347 AA; 37068 MW; 74B76C183F6CB62A CRC64;
MAVFNHPEFD QHEQVVFCSD QETGLKAIIA VHSTRLGPAV GGCRLWDYAS DEDALVDVLR
LSRGMTYKNA MAGLPLGGGK SVIIGNAKTI KSEALFQAFG RMVHRLSGSY YSAEDVNITT
HDIMQVHQVT PYVAGLEGKS GNPGPFTALG TYQGIKAAAK HQFGSADLAG KTVAVQGLGS
VGFYLCEHLH KEGAKLIVTD INQDAVNRAV TQFGATAVGL NDIYGVAADI YAPCALGATL
NDDTIPQLKA KIVAGCANNQ LKRPEHGQKL RELGILYAPD YVINAGGIIN VAFEMRPQGY
NAAESTAKVM QIFDTLLQIF ERADAENKPT STVADQMAQE IIARGQA
//
