ID A0A0B0EMW2_9BACT Unreviewed; 296 AA.
AC A0A0B0EMW2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:KHE92493.1};
DE EC=1.4.1.3 {ECO:0000313|EMBL:KHE92493.1};
GN Name=gdh {ECO:0000313|EMBL:KHE92493.1};
GN ORFNames=SCABRO_01753 {ECO:0000313|EMBL:KHE92493.1};
OS Candidatus Scalindua brodae.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Scalinduaceae; Scalindua.
OX NCBI_TaxID=237368 {ECO:0000313|EMBL:KHE92493.1, ECO:0000313|Proteomes:UP000030652};
RN [1] {ECO:0000313|EMBL:KHE92493.1, ECO:0000313|Proteomes:UP000030652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU1 {ECO:0000313|EMBL:KHE92493.1};
RA Speth D.R., Russ L., Kartal B., Op den Camp H.J., Dutilh B.E., Jetten M.S.;
RT "Draft genome of anammox bacterium scalindua brodae, obtained using
RT differential coverage binning of sequence data from two enrichment
RT reactors.";
RL Submitted (OCT-2014) 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:KHE92493.1}.
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DR EMBL; JRYO01000124; KHE92493.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B0EMW2; -.
DR PATRIC; fig|237368.3.peg.1906; -.
DR eggNOG; COG0334; Bacteria.
DR Proteomes; UP000030652; Unassembled WGS sequence.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11606:SF13; GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR Pfam; PF02812; ELFV_dehydrog_N; 1.
DR PRINTS; PR00082; GLFDHDRGNASE.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417}.
FT DOMAIN 67..194
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02812"
FT DOMAIN 215..280
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00208"
SQ SEQUENCE 296 AA; 32791 MW; 0EAF7D15CF692052 CRC64;
MPFLFFHYSE YLKGSTISST VKAGNPIDNI MKTVLPFFEQ VNFNFDKAAK YTNYSPGILN
EIKICNSVYH MTFPLKRDNG TIETIHAWRA EHSHHKLPTK GGIRYSTLVN EDEIMALAAL
MTYKCAIVDV PFGGAKGGIQ INVEKYSVGE LERITRRYAY ELVSKNFIGP GIDVPAPDYG
TGEREMAWIL DTYTAMTSDK LEARACVTGK PVEQGGIHGR KEATGLGVYY GLREACSFEE
DMKPLGLSSG LEGKSIVVQG FGNVGYHSAK FLQEGGAVIM LSQNLMAPST TLRDWR
//
