ID A0A1S1MW87_9GAMM Unreviewed; 346 AA.
AC A0A1S1MW87;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Amino acid dehydrogenase {ECO:0000313|EMBL:OHU91158.1};
GN ORFNames=BET10_09935 {ECO:0000313|EMBL:OHU91158.1};
OS Pseudoalteromonas amylolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1859457 {ECO:0000313|EMBL:OHU91158.1, ECO:0000313|Proteomes:UP000179786};
RN [1] {ECO:0000313|EMBL:OHU91158.1, ECO:0000313|Proteomes:UP000179786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JW1 {ECO:0000313|EMBL:OHU91158.1,
RC ECO:0000313|Proteomes:UP000179786};
RA Wu Y.-H., Cheng H., Jin X.-B., Wang C.-S., Xu X.-W.;
RT "Pseudoalteromonas amylolytica sp. nov., isolated from the surface
RT seawater.";
RL Submitted (SEP-2016) 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:OHU91158.1}.
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; MKJU01000025; OHU91158.1; -; Genomic_DNA.
DR RefSeq; WP_070984804.1; NZ_MKJU01000025.1.
DR AlphaFoldDB; A0A1S1MW87; -.
DR STRING; 1859457.BET10_09935; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000179786; 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; 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}.
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 346 AA; 37386 MW; F2965C5CD854D93D CRC64;
MAVFNQVEFD NHEQVVFCAD EASGLRAIIA VHSTKLGPAV GGCRLWDYAK DEDAVYDVLR
LSKGMTYKNA VARLPFGGGK SVIIGDAKEI KSEALFRAFG KHLERLGGSY YSAEDVNITT
GDVMMMHKET NYVLGLEGKS GNPSPFTALG TFLGIKAAYQ HKHGHQDLAG VKVAVQGLGA
VAYGLCKHLH EAGAQLFVTD INQASIDRVV SEFGATAVGI DEIYDLDVDV YAPCALGATL
NDNTIPRLKA TVIAGCANNQ LAESRHGEIL REKGVLYAPD YVINAGGIIN VYYETKPEGY
NKEQATKHVE GIYDTLTEIF ARSESEQKST HIIADELAQE IIAQGL
//
