ID V4P6A0_9CAUL Unreviewed; 357 AA.
AC V4P6A0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase C-terminal domain-containing protein {ECO:0000259|SMART:SM00839};
GN ORFNames=AEAC466_15960 {ECO:0000313|EMBL:ESQ82634.1};
OS Asticcacaulis sp. AC466.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282362 {ECO:0000313|EMBL:ESQ82634.1, ECO:0000313|Proteomes:UP000017826};
RN [1] {ECO:0000313|EMBL:ESQ82634.1, ECO:0000313|Proteomes:UP000017826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC466 {ECO:0000313|EMBL:ESQ82634.1,
RC ECO:0000313|Proteomes:UP000017826};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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:ESQ82634.1}.
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DR EMBL; AWGE01000017; ESQ82634.1; -; Genomic_DNA.
DR RefSeq; WP_023459183.1; NZ_AWGE01000017.1.
DR AlphaFoldDB; V4P6A0; -.
DR STRING; 1282362.AEAC466_15960; -.
DR PATRIC; fig|1282362.3.peg.3154; -.
DR eggNOG; COG0334; Bacteria.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000017826; 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:UP000017826}.
FT DOMAIN 143..351
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 179..184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 357 AA; 36703 MW; 20754907708F145D CRC64;
MFDHPDYDGH EKVLMVEDAA SGLKAIIAVH STALGAAAGG CRLWRYESGV SALGDALRLS
RGMSYKNAMA NLPMGGGKAV ILGPVPADRR EAVLEAFGRA VESLDGQYIT AEDVGVSVAD
MKVVSRTTGY VSGLDAAVGK SGGDPSPFTA RGVRVGIEAA VKARLGRSDL AGLTVAVQGL
GHVGTYLCEE LFNLGAKLTV ADINPDRVEE VCARFAAESV SVNDILLQPV DVVAPCALGG
AITEDVASRL QARVVAGAAN NQLLTPGAGI ILGDRGILYA PDYVINAGGI IMVAGEISGN
NDEADILAQV DAIGPRLADI FARAKTENVI TNLVADSMAK DKIASAGRAK ARHAEAA
//
