ID B2IEJ1_BEII9 Unreviewed; 549 AA.
AC B2IEJ1;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Response regulator receiver protein {ECO:0000313|EMBL:ACB95584.1};
GN OrderedLocusNames=Bind_1961 {ECO:0000313|EMBL:ACB95584.1};
OS Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB
OS 8712).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Beijerinckia.
OX NCBI_TaxID=395963 {ECO:0000313|EMBL:ACB95584.1, ECO:0000313|Proteomes:UP000001695};
RN [1] {ECO:0000313|Proteomes:UP000001695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712
RC {ECO:0000313|Proteomes:UP000001695};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N.,
RA Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.;
RT "Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC
RT 9039.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACB95584.1, ECO:0000313|Proteomes:UP000001695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712
RC {ECO:0000313|Proteomes:UP000001695};
RX PubMed=20601475; DOI=10.1128/JB.00656-10;
RA Tamas I., Dedysh S.N., Liesack W., Stott M.B., Alam M., Murrell J.C.,
RA Dunfield P.F.;
RT "Complete genome sequence of Beijerinckia indica subsp. indica.";
RL J. Bacteriol. 192:4532-4533(2010).
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382}.
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DR EMBL; CP001016; ACB95584.1; -; Genomic_DNA.
DR RefSeq; WP_012384940.1; NC_010581.1.
DR AlphaFoldDB; B2IEJ1; -.
DR STRING; 395963.Bind_1961; -.
DR KEGG; bid:Bind_1961; -.
DR eggNOG; COG0334; Bacteria.
DR eggNOG; COG2197; Bacteria.
DR HOGENOM; CLU_025763_1_2_5; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000001695; Chromosome.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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 Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00082; GLFDHDRGNASE.
DR SMART; SM00839; ELFV_dehydrog; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000001695}.
FT DOMAIN 7..124
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 59
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 549 AA; 60111 MW; C1A71042B436B097 CRC64;
MVDHPVRLLL VEDNPLHVKL VLRFLAGDVQ LRCAVEVVDC LSDGLARLGR GALDLVLLDL
ILPDSQELET LFKVRAAAPD TPVIVLTSMD DVKLAARAVD VGAYAYLLKT QINAVSLGRA
IRYTLARART RGNEWDSPIF RLAQQQFLKA AQIMNLDDNF RQRLLFPERT QVVSFPFIRD
DQQQVETVFG YRVQHVLSMG PTKGGIRYHQ DVGLGDVAAL STWMTWKCAL MKLPFGGAKG
GVRIDPTGLS NRELQRLTRR YTSEIINIIG PEKDIPAPDM GTNEQVMAWV MDTYSQQMGY
AVPAVVTGKP VVLGGSLGRK EATGRGLVYL VQAAAQHIGL DLKEATAVVQ GFGNVGSFTV
QFLAETGVKI IGVSDVSTGL YNPAGLSVEA LLKYVATNRE LKGFPDAEPI SNAELLELEC
DVLAVAALQN QITAENAERI HCRLLAEGAN GPTTLEADDV LNARGVFVLP DILANAGGVT
VSYFEWVQGT QNLTWTLEEI NQRLKAILLD AFQRTLHRAE TDKLDMRTAA LIEGVSRVTE
AKRLRGVFP
//
